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</a> <button aria-controls="toc-Models-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Models subsection</span> </button> <ul id="toc-Models-sublist" class="vector-toc-list"> <li id="toc-Concerted_model" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Concerted_model"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.1</span> <span>Concerted model</span> </div> </a> <ul id="toc-Concerted_model-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Sequential_model" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Sequential_model"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2</span> <span>Sequential model</span> </div> </a> <ul id="toc-Sequential_model-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Morpheein_model" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Morpheein_model"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.3</span> <span>Morpheein model</span> </div> </a> <ul id="toc-Morpheein_model-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Ensemble_models" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Ensemble_models"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.4</span> <span>Ensemble models</span> </div> </a> <ul id="toc-Ensemble_models-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Allosteric_modulation" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Allosteric_modulation"> <div class="vector-toc-text"> <span class="vector-toc-numb">3</span> <span>Allosteric modulation</span> </div> </a> <ul id="toc-Allosteric_modulation-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Energy_sensing_model" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Energy_sensing_model"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>Energy sensing model</span> </div> </a> <button aria-controls="toc-Energy_sensing_model-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Energy sensing model subsection</span> </button> <ul id="toc-Energy_sensing_model-sublist" class="vector-toc-list"> <li id="toc-Positive_modulation" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Positive_modulation"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.1</span> <span>Positive modulation</span> </div> </a> <ul id="toc-Positive_modulation-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Negative_modulation" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Negative_modulation"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.2</span> <span>Negative modulation</span> </div> </a> <ul id="toc-Negative_modulation-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Types" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Types"> <div class="vector-toc-text"> <span class="vector-toc-numb">5</span> <span>Types</span> </div> </a> <button aria-controls="toc-Types-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Types subsection</span> </button> <ul id="toc-Types-sublist" class="vector-toc-list"> <li id="toc-Homotropic" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Homotropic"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.1</span> <span>Homotropic</span> </div> </a> <ul id="toc-Homotropic-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Heterotropic" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Heterotropic"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.2</span> <span>Heterotropic</span> </div> </a> <ul id="toc-Heterotropic-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Essential_activators" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Essential_activators"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.3</span> <span>Essential activators</span> </div> </a> <ul id="toc-Essential_activators-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Non-regulatory_allostery" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Non-regulatory_allostery"> <div class="vector-toc-text"> <span class="vector-toc-numb">6</span> <span>Non-regulatory allostery</span> </div> </a> <ul id="toc-Non-regulatory_allostery-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Pharmacology" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Pharmacology"> <div class="vector-toc-text"> <span class="vector-toc-numb">7</span> <span>Pharmacology</span> </div> </a> <button aria-controls="toc-Pharmacology-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Pharmacology subsection</span> </button> <ul id="toc-Pharmacology-sublist" class="vector-toc-list"> <li id="toc-Allosteric_sites_as_drug_targets" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Allosteric_sites_as_drug_targets"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.1</span> <span>Allosteric sites as drug targets</span> </div> </a> <ul id="toc-Allosteric_sites_as_drug_targets-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Synthetic_allosteric_systems" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Synthetic_allosteric_systems"> <div class="vector-toc-text"> <span class="vector-toc-numb">8</span> <span>Synthetic allosteric systems</span> </div> </a> <ul id="toc-Synthetic_allosteric_systems-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Online_resources" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Online_resources"> <div class="vector-toc-text"> <span class="vector-toc-numb">9</span> <span>Online resources</span> </div> </a> <button aria-controls="toc-Online_resources-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Online resources subsection</span> </button> <ul id="toc-Online_resources-sublist" class="vector-toc-list"> <li id="toc-Allosteric_Database" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Allosteric_Database"> <div class="vector-toc-text"> <span class="vector-toc-numb">9.1</span> <span>Allosteric Database</span> </div> </a> <ul id="toc-Allosteric_Database-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Allosteric_residues_and_their_prediction" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Allosteric_residues_and_their_prediction"> <div class="vector-toc-text"> <span class="vector-toc-numb">9.2</span> <span>Allosteric residues and their prediction</span> </div> </a> <ul id="toc-Allosteric_residues_and_their_prediction-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> <span class="vector-toc-numb">10</span> <span>See also</span> </div> </a> <ul id="toc-See_also-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> <span class="vector-toc-numb">11</span> <span>References</span> </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-External_links" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> <span class="vector-toc-numb">12</span> <span>External links</span> </div> </a> <ul id="toc-External_links-sublist" class="vector-toc-list"> </ul> </li> </ul> </div> </div> </nav> </div> </div> <div class="mw-content-container"> <main id="content" class="mw-body"> <header class="mw-body-header vector-page-titlebar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-page-titlebar-toc" class="vector-dropdown vector-page-titlebar-toc vector-button-flush-left" > <input type="checkbox" id="vector-page-titlebar-toc-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-titlebar-toc" class="vector-dropdown-checkbox " aria-label="Toggle the table of contents" > <label id="vector-page-titlebar-toc-label" for="vector-page-titlebar-toc-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" ><span class="vector-icon mw-ui-icon-listBullet mw-ui-icon-wikimedia-listBullet"></span> <span class="vector-dropdown-label-text">Toggle the table of contents</span> </label> <div class="vector-dropdown-content"> <div id="vector-page-titlebar-toc-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Allosteric regulation</span></h1> <div id="p-lang-btn" class="vector-dropdown mw-portlet mw-portlet-lang" > <input type="checkbox" id="p-lang-btn-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-p-lang-btn" class="vector-dropdown-checkbox mw-interlanguage-selector" aria-label="Go to an article in another language. Available in 24 languages" > <label id="p-lang-btn-label" for="p-lang-btn-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--action-progressive mw-portlet-lang-heading-24" aria-hidden="true" ><span class="vector-icon mw-ui-icon-language-progressive mw-ui-icon-wikimedia-language-progressive"></span> <span class="vector-dropdown-label-text">24 languages</span> </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-ar mw-list-item"><a href="https://ar.wikipedia.org/wiki/%D8%AA%D9%81%D8%A7%D8%B1%D8%BA%D9%8A%D8%A9" title="تفارغية – Arabic" lang="ar" hreflang="ar" data-title="تفارغية" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target"><span>العربية</span></a></li><li class="interlanguage-link interwiki-bs mw-list-item"><a href="https://bs.wikipedia.org/wiki/Alosterna_regulacija" title="Alosterna regulacija – Bosnian" lang="bs" hreflang="bs" data-title="Alosterna regulacija" data-language-autonym="Bosanski" data-language-local-name="Bosnian" class="interlanguage-link-target"><span>Bosanski</span></a></li><li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/Regulaci%C3%B3_al%C2%B7lost%C3%A8rica" title="Regulació al·lostèrica – Catalan" lang="ca" hreflang="ca" data-title="Regulació al·lostèrica" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target"><span>Català</span></a></li><li class="interlanguage-link interwiki-cs mw-list-item"><a href="https://cs.wikipedia.org/wiki/Alosterick%C3%A1_regulace" title="Alosterická regulace – Czech" lang="cs" hreflang="cs" data-title="Alosterická regulace" data-language-autonym="Čeština" data-language-local-name="Czech" class="interlanguage-link-target"><span>Čeština</span></a></li><li class="interlanguage-link interwiki-da mw-list-item"><a href="https://da.wikipedia.org/wiki/Allosterisk_regulering" title="Allosterisk regulering – Danish" lang="da" hreflang="da" data-title="Allosterisk regulering" data-language-autonym="Dansk" data-language-local-name="Danish" class="interlanguage-link-target"><span>Dansk</span></a></li><li class="interlanguage-link interwiki-et mw-list-item"><a href="https://et.wikipedia.org/wiki/Allosteeriline_regulatsioon" title="Allosteeriline regulatsioon – Estonian" lang="et" hreflang="et" data-title="Allosteeriline regulatsioon" data-language-autonym="Eesti" data-language-local-name="Estonian" class="interlanguage-link-target"><span>Eesti</span></a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/Regulaci%C3%B3n_alost%C3%A9rica" title="Regulación alostérica – Spanish" lang="es" hreflang="es" data-title="Regulación alostérica" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target"><span>Español</span></a></li><li class="interlanguage-link interwiki-fa mw-list-item"><a href="https://fa.wikipedia.org/wiki/%D8%AA%D9%86%D8%B8%DB%8C%D9%85_%D8%A2%D9%84%D9%88%D8%B3%D8%AA%D8%B1%DB%8C%DA%A9" title="تنظیم آلوستریک – Persian" lang="fa" hreflang="fa" data-title="تنظیم آلوستریک" data-language-autonym="فارسی" data-language-local-name="Persian" class="interlanguage-link-target"><span>فارسی</span></a></li><li class="interlanguage-link interwiki-ko mw-list-item"><a href="https://ko.wikipedia.org/wiki/%EB%8B%A4%EB%A5%B8_%EC%9E%90%EB%A6%AC_%EC%9E%85%EC%B2%B4%EC%84%B1_%EC%A1%B0%EC%A0%88" title="다른 자리 입체성 조절 – Korean" lang="ko" hreflang="ko" data-title="다른 자리 입체성 조절" data-language-autonym="한국어" data-language-local-name="Korean" class="interlanguage-link-target"><span>한국어</span></a></li><li class="interlanguage-link interwiki-hy mw-list-item"><a href="https://hy.wikipedia.org/wiki/%D4%B1%D5%AC%D5%B8%D5%BD%D5%BF%D5%A5%D6%80%D5%AB%D5%AF_%D5%AF%D5%A1%D6%80%D5%A3%D5%A1%D5%BE%D5%B8%D6%80%D5%B8%D6%82%D5%B4" title="Ալոստերիկ կարգավորում – Armenian" lang="hy" hreflang="hy" data-title="Ալոստերիկ կարգավորում" data-language-autonym="Հայերեն" data-language-local-name="Armenian" class="interlanguage-link-target"><span>Հայերեն</span></a></li><li class="interlanguage-link interwiki-id mw-list-item"><a href="https://id.wikipedia.org/wiki/Regulasi_alosterik" title="Regulasi alosterik – Indonesian" lang="id" hreflang="id" data-title="Regulasi alosterik" data-language-autonym="Bahasa Indonesia" data-language-local-name="Indonesian" class="interlanguage-link-target"><span>Bahasa Indonesia</span></a></li><li class="interlanguage-link interwiki-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Regolazione_allosterica" title="Regolazione allosterica – Italian" lang="it" hreflang="it" data-title="Regolazione allosterica" data-language-autonym="Italiano" data-language-local-name="Italian" class="interlanguage-link-target"><span>Italiano</span></a></li><li class="interlanguage-link interwiki-ja mw-list-item"><a href="https://ja.wikipedia.org/wiki/%E3%82%A2%E3%83%AD%E3%82%B9%E3%83%86%E3%83%AA%E3%83%83%E3%82%AF%E5%8A%B9%E6%9E%9C" title="アロステリック効果 – Japanese" lang="ja" hreflang="ja" data-title="アロステリック効果" data-language-autonym="日本語" data-language-local-name="Japanese" class="interlanguage-link-target"><span>日本語</span></a></li><li class="interlanguage-link interwiki-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Inhibicja_allosteryczna" title="Inhibicja allosteryczna – Polish" lang="pl" hreflang="pl" data-title="Inhibicja allosteryczna" data-language-autonym="Polski" data-language-local-name="Polish" class="interlanguage-link-target"><span>Polski</span></a></li><li class="interlanguage-link interwiki-pt mw-list-item"><a href="https://pt.wikipedia.org/wiki/Controle_alost%C3%A9rico" title="Controle alostérico – Portuguese" lang="pt" hreflang="pt" data-title="Controle alostérico" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target"><span>Português</span></a></li><li class="interlanguage-link interwiki-ro mw-list-item"><a href="https://ro.wikipedia.org/wiki/Reglare_alosteric%C4%83" title="Reglare alosterică – Romanian" lang="ro" hreflang="ro" data-title="Reglare alosterică" data-language-autonym="Română" data-language-local-name="Romanian" class="interlanguage-link-target"><span>Română</span></a></li><li class="interlanguage-link interwiki-ru mw-list-item"><a href="https://ru.wikipedia.org/wiki/%D0%90%D0%BB%D0%BB%D0%BE%D1%81%D1%82%D0%B5%D1%80%D0%B8%D1%87%D0%B5%D1%81%D0%BA%D0%B0%D1%8F_%D1%80%D0%B5%D0%B3%D1%83%D0%BB%D1%8F%D1%86%D0%B8%D1%8F" title="Аллостерическая регуляция – Russian" lang="ru" hreflang="ru" data-title="Аллостерическая регуляция" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target"><span>Русский</span></a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/Alosterna_regulacija" title="Alosterna regulacija – Serbian" lang="sr" hreflang="sr" data-title="Alosterna regulacija" data-language-autonym="Српски / srpski" data-language-local-name="Serbian" class="interlanguage-link-target"><span>Српски / srpski</span></a></li><li class="interlanguage-link interwiki-sh mw-list-item"><a href="https://sh.wikipedia.org/wiki/Alosterna_regulacija" title="Alosterna regulacija – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Alosterna regulacija" data-language-autonym="Srpskohrvatski / српскохрватски" data-language-local-name="Serbo-Croatian" class="interlanguage-link-target"><span>Srpskohrvatski / српскохрватски</span></a></li><li class="interlanguage-link interwiki-fi mw-list-item"><a href="https://fi.wikipedia.org/wiki/Allosteerinen_s%C3%A4%C3%A4tely" title="Allosteerinen säätely – Finnish" lang="fi" hreflang="fi" data-title="Allosteerinen säätely" data-language-autonym="Suomi" data-language-local-name="Finnish" class="interlanguage-link-target"><span>Suomi</span></a></li><li class="interlanguage-link interwiki-sv mw-list-item"><a href="https://sv.wikipedia.org/wiki/Alloster_reglering" title="Alloster reglering – Swedish" lang="sv" hreflang="sv" data-title="Alloster reglering" data-language-autonym="Svenska" data-language-local-name="Swedish" class="interlanguage-link-target"><span>Svenska</span></a></li><li class="interlanguage-link interwiki-th mw-list-item"><a href="https://th.wikipedia.org/wiki/%E0%B8%81%E0%B8%B2%E0%B8%A3%E0%B8%84%E0%B8%A7%E0%B8%9A%E0%B8%84%E0%B8%B8%E0%B8%A1%E0%B9%81%E0%B8%9A%E0%B8%9A%E0%B8%AD%E0%B8%B1%E0%B8%A5%E0%B9%82%E0%B8%A5%E0%B8%AA%E0%B9%80%E0%B8%95%E0%B8%AD%E0%B8%A3%E0%B8%B4%E0%B8%81" title="การควบคุมแบบอัลโลสเตอริก – Thai" lang="th" hreflang="th" data-title="การควบคุมแบบอัลโลสเตอริก" data-language-autonym="ไทย" data-language-local-name="Thai" class="interlanguage-link-target"><span>ไทย</span></a></li><li class="interlanguage-link interwiki-tr mw-list-item"><a href="https://tr.wikipedia.org/wiki/Allosterik_d%C3%BCzenleme" title="Allosterik düzenleme – Turkish" lang="tr" hreflang="tr" data-title="Allosterik düzenleme" data-language-autonym="Türkçe" data-language-local-name="Turkish" class="interlanguage-link-target"><span>Türkçe</span></a></li><li class="interlanguage-link interwiki-zh mw-list-item"><a href="https://zh.wikipedia.org/wiki/%E5%88%AB%E6%9E%84%E8%B0%83%E8%8A%82" title="别构调节 – Chinese" lang="zh" hreflang="zh" data-title="别构调节" data-language-autonym="中文" data-language-local-name="Chinese" class="interlanguage-link-target"><span>中文</span></a></li> </ul> <div class="after-portlet after-portlet-lang"><span class="wb-langlinks-edit wb-langlinks-link"><a href="https://www.wikidata.org/wiki/Special:EntityPage/Q845326#sitelinks-wikipedia" title="Edit interlanguage links" class="wbc-editpage">Edit links</a></span></div> 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dir="ltr"><div class="shortdescription nomobile noexcerpt noprint searchaux" style="display:none">Regulation of enzyme activity</div> <p class="mw-empty-elt"> </p> <figure class="mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Enzyme_Model.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/e/e7/Enzyme_Model.svg/300px-Enzyme_Model.svg.png" decoding="async" width="300" height="300" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/e/e7/Enzyme_Model.svg/450px-Enzyme_Model.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/e/e7/Enzyme_Model.svg/600px-Enzyme_Model.svg.png 2x" data-file-width="177" data-file-height="177" /></a><figcaption>Allosteric regulation of an enzyme</figcaption></figure> <p>In the fields of <a href="/wiki/Biochemistry" title="Biochemistry">biochemistry</a> and <a href="/wiki/Pharmacology" title="Pharmacology">pharmacology</a> an <b>allosteric regulator</b> (or <b>allosteric modulator</b>) is a substance that binds to a site on an <a href="/wiki/Enzyme" title="Enzyme">enzyme</a> or <a href="/wiki/Receptor_(biochemistry)" title="Receptor (biochemistry)">receptor</a> distinct from the <a href="/wiki/Active_site" title="Active site">active site</a>, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function. In contrast, substances that bind directly to an enzyme's active site or the binding site of the <a href="/wiki/Endogenous_ligand" class="mw-redirect" title="Endogenous ligand">endogenous ligand</a> of a receptor are called <b>orthosteric</b> regulators or modulators. </p><p>The site to which the effector binds is termed the <i>allosteric site</i> or <i>regulatory site</i>. Allosteric sites allow effectors to bind to the protein, often resulting in a <a href="/wiki/Conformational_change" title="Conformational change">conformational change</a> and/or a change in <a href="/wiki/Protein_dynamics" title="Protein dynamics">protein dynamics</a>.<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-2" class="reference"><a href="#cite_note-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> Effectors that enhance the protein's activity are referred to as <i>allosteric activators</i>, whereas those that decrease the protein's activity are called <i>allosteric inhibitors</i>. </p><p>Allosteric regulations are a natural example of control loops, such as <a href="/wiki/Feedback#Biology" title="Feedback">feedback</a> from downstream products or <a href="/wiki/Feed_forward_(control)" title="Feed forward (control)">feedforward</a> from upstream substrates. Long-range allostery is especially important in <a href="/wiki/Cell_signaling" title="Cell signaling">cell signaling</a>.<sup id="cite_ref-pmid21570668_3-0" class="reference"><a href="#cite_note-pmid21570668-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> Allosteric regulation is also particularly important in the <a href="/wiki/Cell_(biology)" title="Cell (biology)">cell's</a> ability to adjust <a href="/wiki/Enzyme" title="Enzyme">enzyme</a> activity. </p><p>The term <i>allostery</i> comes from the <a href="/wiki/Ancient_Greek" title="Ancient Greek">Ancient Greek</a> <i>allos</i> (<span lang="grc"><a href="https://en.wiktionary.org/wiki/%E1%BC%84%CE%BB%CE%BB%CE%BF%CF%82#Ancient_Greek" class="extiw" title="wikt:ἄλλος">ἄλλος</a></span>), "other", and <i>stereos</i> (<span lang="grc"><a href="https://en.wiktionary.org/wiki/%CF%83%CF%84%CE%B5%CF%81%CE%B5%CF%8C%CF%82#Ancient_Greek" class="extiw" title="wikt:στερεός">στερεός</a></span>), "solid (object)". This is in reference to the fact that the regulatory site of an allosteric protein is physically distinct from its active site. Allostery contrasts with <a href="/wiki/Substrate_presentation" title="Substrate presentation">substrate presentation</a> which requires no conformational change for an enzyme's activation. The term <i>orthostery</i> comes from the <a href="/wiki/Ancient_Greek" title="Ancient Greek">Ancient Greek</a> orthós (<span lang="grc"><a href="https://en.wiktionary.org/wiki/%E1%BD%80%CF%81%CE%B8%CF%8C%CF%82#Ancient_Greek" class="extiw" title="wikt:ὀρθός">ὀρθός</a></span>) meaning “straight”, “upright”, “right” or “correct”. </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Ortho_vs._allosteric_inhibitors">Ortho vs. allosteric inhibitors</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=1" title="Edit section: Ortho vs. allosteric inhibitors"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Orthosteric">Orthosteric</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=2" title="Edit section: Orthosteric"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ol><li>Binding Site: Orthosteric inhibitors bind directly to the enzyme's active site, where the substrate normally binds.</li> <li>Mechanism of Action: By occupying the active site, these inhibitors prevent the substrate from binding, thereby directly blocking the enzyme's catalytic activity.</li> <li>Competitive Inhibition: Most orthosteric inhibitors compete with the substrate for the active site, which means their effectiveness can be reduced if substrate concentration increases.</li></ol> <div class="mw-heading mw-heading3"><h3 id="Allosteric">Allosteric</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=3" title="Edit section: Allosteric"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ol><li>Binding Site: Allosteric inhibitors bind to a site on the enzyme that is distinct and separate from the active site, known as the allosteric site.</li> <li>Mechanism of Action: Binding to the allosteric site induces a conformational change in the enzyme that can either reduce the affinity of the active site for the substrate or alter the enzyme's catalytic activity. This indirect interference can inhibit the enzyme's function even if the substrate is present.</li> <li>Non-Competitive Inhibition: Allosteric inhibitors often exhibit non-competitive inhibition, meaning their inhibitory effect is not dependent on the substrate concentration.</li></ol> <div class="mw-heading mw-heading2"><h2 id="Models">Models</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=4" title="Edit section: Models"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Allosteric_Regulation.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/4/47/Allosteric_Regulation.svg/220px-Allosteric_Regulation.svg.png" decoding="async" width="220" height="165" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/4/47/Allosteric_Regulation.svg/330px-Allosteric_Regulation.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/4/47/Allosteric_Regulation.svg/440px-Allosteric_Regulation.svg.png 2x" data-file-width="512" data-file-height="384" /></a><figcaption>A – <a href="/wiki/Active_site" title="Active site">Active site</a><br /> B – Allosteric site<br /> C – <a href="/wiki/Substrate_(biochemistry)" class="mw-redirect" title="Substrate (biochemistry)">Substrate</a><br /> D – <a href="/wiki/Enzyme_inhibitor" title="Enzyme inhibitor">Inhibitor</a><br /> E – <a href="/wiki/Enzyme" title="Enzyme">Enzyme</a><br />This is a diagram of allosteric regulation of an enzyme.</figcaption></figure> <p>Many allosteric effects can be explained by the <i>concerted</i> <a href="/wiki/MWC_model" class="mw-redirect" title="MWC model">MWC model</a> put forth by <a href="/wiki/Jacques_Monod" title="Jacques Monod">Monod</a>, <a href="/wiki/Jeffries_Wyman_(biologist)" title="Jeffries Wyman (biologist)">Wyman</a>, and <a href="/wiki/Jean-Pierre_Changeux" title="Jean-Pierre Changeux">Changeux</a>,<sup id="cite_ref-pmid14343300_4-0" class="reference"><a href="#cite_note-pmid14343300-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> or by the <a href="/wiki/Sequential_model" title="Sequential model">sequential model</a> (also known as the KNF model) described by <a href="/wiki/Daniel_E._Koshland_Jr." title="Daniel E. Koshland Jr.">Koshland</a>, Nemethy, and Filmer.<sup id="cite_ref-pmid5938952_5-0" class="reference"><a href="#cite_note-pmid5938952-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> Both postulate that <a href="/wiki/Protein_subunit" title="Protein subunit">protein subunits</a> exist in one of two <a href="/wiki/Protein_structure" title="Protein structure">conformations</a>, tensed (T) or relaxed (R), and that relaxed subunits bind substrate more readily than those in the tense state. The two models differ most in their assumptions about subunit interaction and the preexistence of both states. For proteins in which <a href="/wiki/Protein_subunit" title="Protein subunit">subunits</a> exist in more than two <a href="/wiki/Protein_structure" title="Protein structure">conformations</a>, the allostery landscape model described by Cuendet, Weinstein, and LeVine,<sup id="cite_ref-Cuendet_2016_6-0" class="reference"><a href="#cite_note-Cuendet_2016-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> can be used. Allosteric regulation may be facilitated by the evolution of large-scale, low-energy conformational changes, which enables long-range allosteric interaction between distant binding sites.<sup id="cite_ref-7" class="reference"><a href="#cite_note-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Concerted_model">Concerted model</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=5" title="Edit section: Concerted model"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The concerted model of allostery, also referred to as the symmetry model or <a href="/wiki/MWC_model" class="mw-redirect" title="MWC model">MWC model</a>, postulates that enzyme subunits are connected in such a way that a conformational change in one subunit is necessarily conferred to all other subunits. Thus, all subunits must exist in the same conformation. The model further holds that, in the absence of any ligand (substrate or otherwise), the equilibrium favors one of the conformational states, T or R. The equilibrium can be shifted to the R or T state through the binding of one <a href="/wiki/Ligand_(biochemistry)" title="Ligand (biochemistry)">ligand</a> (the allosteric effector or ligand) to a site that is different from the active site </p> <div class="mw-heading mw-heading3"><h3 id="Sequential_model">Sequential model</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=6" title="Edit section: Sequential model"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The sequential model of allosteric regulation holds that subunits are not connected in such a way that a conformational change in one induces a similar change in the others. Thus, all enzyme subunits do not necessitate the same conformation. Moreover, the sequential model dictates that molecules of a substrate bind via an <a href="/wiki/Induced_fit" class="mw-redirect" title="Induced fit">induced fit</a> protocol. While such an induced fit converts a subunit from the tensed state to relaxed state, it does not propagate the conformational change to adjacent subunits. Instead, substrate-binding at one subunit only slightly alters the structure of other subunits so that their binding sites are more receptive to substrate. To summarize: </p> <ul><li>subunits need not exist in the same conformation</li> <li>molecules of substrate bind via induced-fit protocol</li> <li>conformational changes are not propagated to all subunits</li></ul> <div class="mw-heading mw-heading3"><h3 id="Morpheein_model">Morpheein model</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=7" title="Edit section: Morpheein model"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/Morpheein" title="Morpheein">morpheein</a> model of allosteric regulation is a dissociative concerted model.<sup id="cite_ref-pmid16023348_8-0" class="reference"><a href="#cite_note-pmid16023348-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> </p><p>A morpheein is a homo-oligomeric structure that can exist as an ensemble of physiologically significant and functionally different alternate quaternary assemblies. Transitions between alternate morpheein assemblies involve oligomer dissociation, conformational change in the dissociated state, and reassembly to a different oligomer. The required oligomer disassembly step differentiates the morpheein model for allosteric regulation from the classic MWC and KNF models. </p><p><a href="/wiki/Porphobilinogen_synthase" class="mw-redirect" title="Porphobilinogen synthase">Porphobilinogen synthase</a> (PBGS) is the prototype morpheein. </p> <div class="mw-heading mw-heading3"><h3 id="Ensemble_models">Ensemble models</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=8" title="Edit section: Ensemble models"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Ensemble models of allosteric regulation enumerate an allosteric system's <a href="/wiki/Statistical_ensemble" class="mw-redirect" title="Statistical ensemble">statistical ensemble</a> as a function of its <a href="/wiki/Energy_functional" class="mw-redirect" title="Energy functional">potential energy function</a>, and then relate specific statistical measurements of allostery to specific energy terms in the energy function (such as an intermolecular salt bridge between two domains).<sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> Ensemble models like the ensemble allosteric model<sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> and allosteric Ising model<sup id="cite_ref-11" class="reference"><a href="#cite_note-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> assume that each domain of the system can adopt two states similar to the MWC model. The allostery landscape model introduced by Cuendet, Weinstein, and LeVine<sup id="cite_ref-Cuendet_2016_6-1" class="reference"><a href="#cite_note-Cuendet_2016-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> allows for the domains to have any number of states and the contribution of a specific molecular interaction to a given allosteric coupling can be estimated using a rigorous set of rules. <a href="/wiki/Molecular_dynamics" title="Molecular dynamics">Molecular dynamics</a> simulations can be used to estimate a system's statistical ensemble so that it can be analyzed with the allostery landscape model. </p> <div class="mw-heading mw-heading2"><h2 id="Allosteric_modulation">Allosteric modulation</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=9" title="Edit section: Allosteric modulation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1236090951">.mw-parser-output .hatnote{font-style:italic}.mw-parser-output div.hatnote{padding-left:1.6em;margin-bottom:0.5em}.mw-parser-output .hatnote i{font-style:normal}.mw-parser-output .hatnote+link+.hatnote{margin-top:-0.5em}@media print{body.ns-0 .mw-parser-output .hatnote{display:none!important}}</style><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Allosteric_modulator" title="Allosteric modulator">Allosteric modulator</a></div> <p><a href="/wiki/Allosteric_modulation" class="mw-redirect" title="Allosteric modulation">Allosteric modulation</a> is used to alter the activity of molecules and enzymes in biochemistry and pharmacology. For comparison, a typical drug is made to bind to the active site of an enzyme which thus prohibits binding of a substrate to that enzyme causing a decrease in enzyme activity. Allosteric modulation occurs when an <a href="/wiki/Effector_(biology)" title="Effector (biology)">effector</a> binds to an allosteric site (also known as a regulatory site) of an enzyme and alters the enzyme activity. Allosteric modulators are designed to fit the allosteric site to cause a conformational change of the enzyme, in particular a change in the shape of the active site, which then causes a change in its activity. In contrast to typical drugs, modulators are not <a href="/wiki/Competitive_inhibition" title="Competitive inhibition">competitive inhibitors</a>. They can be positive (activating) causing an increase of the enzyme activity or negative (inhibiting) causing a decrease of the enzyme activity. The use of allosteric modulation allows the control of the effects of specific enzyme activities; as a result, allosteric modulators are very effective in pharmacology.<sup id="cite_ref-12" class="reference"><a href="#cite_note-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> In a biological system, allosteric modulation can be difficult to distinguish from modulation by <a href="/wiki/Substrate_presentation" title="Substrate presentation">substrate presentation</a>. </p> <div class="mw-heading mw-heading2"><h2 id="Energy_sensing_model">Energy sensing model</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=10" title="Edit section: Energy sensing model"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>An example of this model is seen with the <i><a href="/wiki/Mycobacterium_tuberculosis" title="Mycobacterium tuberculosis">Mycobacterium tuberculosis</a></i>, a <a href="/wiki/Bacteria" title="Bacteria">bacterium</a> that is perfectly suited to adapt to living in the macrophages of humans. The enzyme's sites serve as a communication between different substrates. Specifically between <a href="/wiki/Adenosine_monophosphate" title="Adenosine monophosphate">AMP</a> and <a href="/wiki/Glucose_6-phosphate" title="Glucose 6-phosphate">G6P</a>. Sites like these also serve as a sensing mechanism for the enzyme's performance.<sup id="cite_ref-pmid29215013_13-0" class="reference"><a href="#cite_note-pmid29215013-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Positive_modulation">Positive modulation</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=11" title="Edit section: Positive modulation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Positive allosteric modulation (also known as <i>allosteric activation</i>) occurs when the binding of one <a href="/wiki/Ligand" title="Ligand">ligand</a> enhances the attraction between substrate molecules and other binding sites. An example is the binding of <a href="/wiki/Oxygen" title="Oxygen">oxygen</a> molecules to <a href="/wiki/Hemoglobin" title="Hemoglobin">hemoglobin</a>, where oxygen is effectively both the <a href="/wiki/Substrate_(biochemistry)" class="mw-redirect" title="Substrate (biochemistry)">substrate</a> and the effector. The allosteric, or "other", site is the <a href="/wiki/Catalytic_site" class="mw-redirect" title="Catalytic site">active site</a> of an adjoining <a href="/wiki/Protein_subunit" title="Protein subunit">protein subunit</a>. The binding of oxygen to one subunit induces a conformational change in that subunit that interacts with the remaining active sites to enhance <i>their</i> oxygen affinity. Another example of allosteric activation is seen in cytosolic IMP-GMP specific 5'-nucleotidase II (cN-II), where the affinity for substrate GMP increases upon GTP binding at the dimer interface. </p> <div class="mw-heading mw-heading3"><h3 id="Negative_modulation">Negative modulation</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=12" title="Edit section: Negative modulation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Negative allosteric modulation (also known as <i>allosteric inhibition</i>) occurs when the binding of one <a href="/wiki/Ligand" title="Ligand">ligand</a> decreases the affinity for substrate at other active sites. For example, when <a href="/wiki/2,3-bisphosphoglycerate" class="mw-redirect" title="2,3-bisphosphoglycerate">2,3-BPG</a> binds to an allosteric site on hemoglobin, the affinity for oxygen of all subunits decreases. This is when a regulator is absent from the binding site. </p><p><a href="/wiki/Direct_thrombin_inhibitors" class="mw-redirect" title="Direct thrombin inhibitors">Direct thrombin inhibitors</a> provides an excellent example of negative allosteric modulation. <a href="/wiki/Direct_thrombin_inhibitors#Allosteric_Inhibitors" class="mw-redirect" title="Direct thrombin inhibitors">Allosteric inhibitors</a> of thrombin have been discovered that could potentially be used as anticoagulants. </p><p>Another example is <a href="/wiki/Strychnine" title="Strychnine">strychnine</a>, a <a href="/wiki/Seizure" title="Seizure">convulsant</a> poison, which acts as an allosteric inhibitor of the <a href="/wiki/Glycine_receptor" title="Glycine receptor">glycine receptor</a>. <a href="/wiki/Glycine" title="Glycine">Glycine</a> is a major post-<a href="/wiki/Synapse" title="Synapse">synaptic</a> inhibitory <a href="/wiki/Neurotransmitter" title="Neurotransmitter">neurotransmitter</a> in <a href="/wiki/Mammal" title="Mammal">mammalian</a> <a href="/wiki/Spinal_cord" title="Spinal cord">spinal cord</a> and <a href="/wiki/Brain_stem" class="mw-redirect" title="Brain stem">brain stem</a>. Strychnine acts at a separate binding site on the glycine receptor in an allosteric manner; i.e., its binding lowers the <a href="/wiki/Affinity_(pharmacology)" class="mw-redirect" title="Affinity (pharmacology)">affinity</a> of the glycine receptor for glycine. Thus, strychnine inhibits the action of an inhibitory transmitter, leading to convulsions. </p><p>Another instance in which negative allosteric modulation can be seen is between <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a> and the enzyme <a href="/wiki/Phosphofructokinase" title="Phosphofructokinase">phosphofructokinase</a> within the <a href="/wiki/Negative_feedback" title="Negative feedback">negative feedback</a> loop that regulates <a href="/wiki/Glycolysis" title="Glycolysis">glycolysis</a>. Phosphofructokinase (generally referred to as <a href="/wiki/PFK" class="mw-redirect" title="PFK">PFK</a>) is an enzyme that catalyses the third step of glycolysis: the <a href="/wiki/Phosphorylation" title="Phosphorylation">phosphorylation</a> of <a href="/wiki/Fructose-6-phosphate" class="mw-redirect" title="Fructose-6-phosphate">fructose-6-phosphate</a> into <a href="/wiki/Fructose_1,6-bisphosphate" title="Fructose 1,6-bisphosphate">fructose 1,6-bisphosphate</a>. <a href="/wiki/PFK" class="mw-redirect" title="PFK">PFK</a> can be allosterically inhibited by high levels of <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a> within the cell. When ATP levels are high, ATP will bind to an allosteric site on <a href="/wiki/Phosphofructokinase" title="Phosphofructokinase">phosphofructokinase</a>, causing a change in the enzyme's three-dimensional shape. This change causes its <a href="/wiki/Affinity_(pharmacology)" class="mw-redirect" title="Affinity (pharmacology)">affinity</a> for <a href="/wiki/Substrate_(biochemistry)" class="mw-redirect" title="Substrate (biochemistry)">substrate</a> (<a href="/wiki/Fructose-6-phosphate" class="mw-redirect" title="Fructose-6-phosphate">fructose-6-phosphate</a> and <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a>) at the active site to decrease, and the enzyme is deemed inactive. This causes <a href="/wiki/Glycolysis" title="Glycolysis">glycolysis</a> to cease when ATP levels are high, thus conserving the body's <a href="/wiki/Glucose" title="Glucose">glucose</a> and maintaining balanced levels of cellular ATP. In this way, ATP serves as a negative allosteric modulator for PFK, despite the fact that it is also a substrate of the enzyme. </p> <div class="mw-heading mw-heading2"><h2 id="Types">Types</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=13" title="Edit section: Types"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Homotropic">Homotropic</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=14" title="Edit section: Homotropic"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>A homotropic allosteric modulator is a <a href="/wiki/Substrate_(biochemistry)" class="mw-redirect" title="Substrate (biochemistry)">substrate</a> for its target <a href="/wiki/Protein" title="Protein">protein</a>, as well as a regulatory molecule of the protein's activity. It is typically an activator of the protein.<sup id="cite_ref-pmid24456211_14-0" class="reference"><a href="#cite_note-pmid24456211-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> For example, O<sub>2</sub> and CO are homotropic allosteric modulators of hemoglobin. Likewise, in IMP/GMP specific 5' nucleotidase, binding of one GMP molecule to a single subunit of the tetrameric enzyme leads to increased affinity for GMP by the subsequent subunits as revealed by sigmoidal substrate versus velocity plots.<sup id="cite_ref-pmid24456211_14-1" class="reference"><a href="#cite_note-pmid24456211-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Heterotropic">Heterotropic</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=15" title="Edit section: Heterotropic"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>A heterotropic allosteric modulator is a regulatory molecule that is not the enzyme's substrate. It may be either an activator or an inhibitor of the enzyme. For example, H<sup>+</sup>, CO<sub>2</sub>, and <a href="/wiki/2,3-bisphosphoglycerate" class="mw-redirect" title="2,3-bisphosphoglycerate">2,3-bisphosphoglycerate</a> are heterotropic allosteric modulators of hemoglobin.<sup id="cite_ref-15" class="reference"><a href="#cite_note-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup> Once again, in IMP/GMP specific 5' nucleotidase, binding of GTP molecule at the dimer interface in the tetrameric enzyme leads to increased affinity for substrate GMP at the active site indicating towards K-type heterotropic allosteric activation.<sup id="cite_ref-pmid24456211_14-2" class="reference"><a href="#cite_note-pmid24456211-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> </p><p>As has been amply highlighted above, some allosteric proteins can be regulated by both their substrates and other molecules. Such proteins are capable of both homotropic and heterotropic interactions.<sup id="cite_ref-pmid24456211_14-3" class="reference"><a href="#cite_note-pmid24456211-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Essential_activators"><span class="anchor" id="Essential_Activators"></span>Essential activators</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=16" title="Edit section: Essential activators"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Some allosteric activators are referred to as "essential", or "obligate" activators, in the sense that in their absence, the activity of their target enzyme activity is very low or negligible, as is the case with N-acetylglutamate's activity on carbamoyl phosphate synthetase I, for example.<sup id="cite_ref-16" class="reference"><a href="#cite_note-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-17" class="reference"><a href="#cite_note-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Non-regulatory_allostery">Non-regulatory allostery</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=17" title="Edit section: Non-regulatory allostery"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>A non-regulatory allosteric site is any non-regulatory component of an enzyme (or any protein), that is not itself an amino acid. For instance, many enzymes require sodium binding to ensure proper function. However, the sodium does not necessarily act as a regulatory subunit; the sodium is always present and there are no known biological processes to add/remove sodium to regulate enzyme activity. Non-regulatory allostery could comprise any other ions besides sodium (calcium, magnesium, zinc), as well as other chemicals and possibly vitamins. </p> <div class="mw-heading mw-heading2"><h2 id="Pharmacology">Pharmacology</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=18" title="Edit section: Pharmacology"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Allosteric modulation of a receptor results from the binding of allosteric modulators at a different site (a "<a href="/wiki/Regulatory_site" class="mw-redirect" title="Regulatory site">regulatory site</a>") from that of the <a href="/wiki/Ligand_(biochemistry)" title="Ligand (biochemistry)">endogenous ligand</a> (an "<a href="/wiki/Active_site" title="Active site">active site</a>") and enhances or inhibits the effects of the endogenous ligand. Under normal circumstances, it acts by causing a <a href="/wiki/Conformational_change" title="Conformational change">conformational change</a> in a receptor molecule, which results in a change in the <a href="/wiki/Dissociation_constant#Protein-ligand_binding" title="Dissociation constant">binding affinity</a> of the ligand. In this way, an allosteric ligand modulates the receptor's activation by its primary <a href="https://en.wiktionary.org/wiki/orthosteric" class="extiw" title="wikt:orthosteric">orthosteric</a> ligand, and can be thought to act like a dimmer switch in an electrical circuit, adjusting the intensity of the response. </p><p>For example, the <a href="/wiki/GABAA_receptor" title="GABAA receptor">GABA<sub>A</sub> receptor</a> has two active sites that the neurotransmitter <a href="/wiki/Gamma-aminobutyric_acid" class="mw-redirect" title="Gamma-aminobutyric acid">gamma-aminobutyric acid</a> (GABA) binds, but also has <a href="/wiki/Benzodiazepine" title="Benzodiazepine">benzodiazepine</a> and <a href="/wiki/General_anaesthetic" title="General anaesthetic">general anaesthetic agent</a> regulatory binding sites. These regulatory sites can each produce positive allosteric modulation, <a href="/wiki/Synergy" title="Synergy">potentiating</a> the activity of GABA. <a href="/wiki/Diazepam" title="Diazepam">Diazepam</a> is a <a href="/wiki/Agonist" title="Agonist">positive allosteric modulator</a> at the benzodiazepine regulatory site, and its antidote <a href="/wiki/Flumazenil" title="Flumazenil">flumazenil</a> is a <a href="/wiki/Receptor_antagonist" title="Receptor antagonist">receptor antagonist</a>. </p><p>More recent examples of drugs that allosterically modulate their targets include the calcium-mimicking <a href="/wiki/Cinacalcet" title="Cinacalcet">cinacalcet</a> and the HIV treatment <a href="/wiki/Maraviroc" title="Maraviroc">maraviroc</a>. </p> <div class="mw-heading mw-heading3"><h3 id="Allosteric_sites_as_drug_targets">Allosteric sites as drug targets</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=19" title="Edit section: Allosteric sites as drug targets"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Allosteric proteins are involved in, and are central in many diseases,<sup id="cite_ref-NC_18-0" class="reference"><a href="#cite_note-NC-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-AAI_19-0" class="reference"><a href="#cite_note-AAI-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> and allosteric sites may represent a novel <a href="/wiki/Drug_discovery#Targets" title="Drug discovery">drug target</a>. There are a number of advantages in using allosteric modulators as preferred therapeutic agents over classic orthosteric ligands. For example, <a href="/wiki/G_protein-coupled_receptor" title="G protein-coupled receptor">G protein-coupled receptor</a> (GPCR) allosteric binding sites have not faced the same evolutionary pressure as <b>orthosteric sites</b> to accommodate an endogenous ligand, so are more diverse.<sup id="cite_ref-AC_20-0" class="reference"><a href="#cite_note-AC-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> Therefore, greater GPCR selectivity may be obtained by targeting allosteric sites.<sup id="cite_ref-AC_20-1" class="reference"><a href="#cite_note-AC-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> This is particularly useful for GPCRs where selective orthosteric therapy has been difficult because of sequence conservation of the orthosteric site across receptor subtypes.<sup id="cite_ref-LM_21-0" class="reference"><a href="#cite_note-LM-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> Also, these modulators have a decreased potential for toxic effects, since modulators with limited co-operativity will have a ceiling level to their effect, irrespective of the administered dose.<sup id="cite_ref-AC_20-2" class="reference"><a href="#cite_note-AC-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> Another type of pharmacological selectivity that is unique to allosteric modulators is based on co-operativity. An allosteric modulator may display neutral co-operativity with an orthosteric ligand at all subtypes of a given receptor except the subtype of interest, which is termed "absolute subtype selectivity".<sup id="cite_ref-LM_21-1" class="reference"><a href="#cite_note-LM-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> If an allosteric modulator does not possess appreciable efficacy, it can provide another powerful therapeutic advantage over orthosteric ligands, namely the ability to selectively tune up or down tissue responses only when the endogenous agonist is present.<sup id="cite_ref-LM_21-2" class="reference"><a href="#cite_note-LM-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> Oligomer-specific small molecule binding sites are drug targets for medically relevant <a href="/wiki/Morpheein" title="Morpheein">morpheeins</a>.<sup id="cite_ref-pmid21643557_22-0" class="reference"><a href="#cite_note-pmid21643557-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Synthetic_allosteric_systems">Synthetic allosteric systems</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=20" title="Edit section: Synthetic allosteric systems"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>There are many synthetic compounds containing several <a href="/wiki/Noncovalent" class="mw-redirect" title="Noncovalent">noncovalent</a> binding sites, which exhibit conformational changes upon occupation of one site. Cooperativity between single binding contributions in such <a href="/wiki/Supramolecular" class="mw-redirect" title="Supramolecular">supramolecular</a> systems is positive if occupation of one binding site enhances the affinity Δ<i>G</i> at a second site, and negative if the affinity isn't highered. Most synthetic allosteric complexes rely on conformational reorganization upon the binding of one effector ligand which then leads to either enhanced or weakened association of second ligand at another binding site.<sup id="cite_ref-23" class="reference"><a href="#cite_note-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-24" class="reference"><a href="#cite_note-24"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-25" class="reference"><a href="#cite_note-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> Conformational coupling between several binding sites is in artificial systems usually much larger than in proteins with their usually larger flexibility. The parameter which determines the efficiency (as measured by the ratio of equilibrium constants Krel = KA(E)/KA in presence and absence of an effector E ) is the conformational energy needed to adopt a closed or strained conformation for the binding of a ligand A.<sup id="cite_ref-26" class="reference"><a href="#cite_note-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> </p><p>In many multivalent <a href="/wiki/Supramolecular" class="mw-redirect" title="Supramolecular">supramolecular</a> systems<sup id="cite_ref-27" class="reference"><a href="#cite_note-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> direct interaction between bound ligands can occur, which can lead to large cooperativities. Most common is such a direct interaction between ions in receptors for ion-pairs.<sup id="cite_ref-28" class="reference"><a href="#cite_note-28"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-29" class="reference"><a href="#cite_note-29"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup> This cooperativity is often also referred to as allostery, even though conformational changes here are not necessarily triggering binding events. </p> <div class="mw-heading mw-heading2"><h2 id="Online_resources">Online resources</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=21" title="Edit section: Online resources"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Allosteric_Database">Allosteric Database</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=22" title="Edit section: Allosteric Database"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Allostery is a direct and efficient means for regulation of biological macromolecule function, produced by the binding of a ligand at an allosteric site topographically distinct from the orthosteric site. Due to the often high receptor selectivity and lower target-based toxicity, allosteric regulation is also expected to play an increasing role in drug discovery and bioengineering. <a rel="nofollow" class="external text" href="http://mdl.shsmu.edu.cn/ASD">The AlloSteric Database</a> (ASD)<sup id="cite_ref-ZH_30-0" class="reference"><a href="#cite_note-ZH-30"><span class="cite-bracket">[</span>30<span class="cite-bracket">]</span></a></sup> provides a central resource for the display, search and analysis of the structure, function and related annotation for allosteric molecules. Currently, ASD contains allosteric proteins from more than 100 species and modulators in three categories (activators, inhibitors, and regulators). Each protein is annotated with detailed description of allostery, biological process and related diseases, and each modulator with binding affinity, physicochemical properties and therapeutic area. Integrating the information of allosteric proteins in ASD should allow the prediction of allostery for unknown proteins, to be followed with experimental validation. In addition, modulators curated in ASD can be used to investigate potential allosteric targets for a query compound, and can help chemists to implement structure modifications for novel allosteric drug design. </p> <div class="mw-heading mw-heading3"><h3 id="Allosteric_residues_and_their_prediction">Allosteric residues and their prediction</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=23" title="Edit section: Allosteric residues and their prediction"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Not all protein residues play equally important roles in allosteric regulation. The identification of residues that are essential to allostery (so-called “allosteric residues”) has been the focus of many studies, especially within the last decade.<sup id="cite_ref-31" class="reference"><a href="#cite_note-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-32" class="reference"><a href="#cite_note-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-33" class="reference"><a href="#cite_note-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-34" class="reference"><a href="#cite_note-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-35" class="reference"><a href="#cite_note-35"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-36" class="reference"><a href="#cite_note-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-37" class="reference"><a href="#cite_note-37"><span class="cite-bracket">[</span>37<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-38" class="reference"><a href="#cite_note-38"><span class="cite-bracket">[</span>38<span class="cite-bracket">]</span></a></sup> In part, this growing interest is a result of their general importance in protein science, but also because allosteric residues may be exploited in <a href="#Allosteric_sites_as_drug_targets">biomedical contexts</a>. Pharmacologically important proteins with difficult-to-target sites may yield to approaches in which one alternatively targets easier-to-reach residues that are capable of allosterically regulating the primary site of interest.<sup id="cite_ref-pmid30530700_39-0" class="reference"><a href="#cite_note-pmid30530700-39"><span class="cite-bracket">[</span>39<span class="cite-bracket">]</span></a></sup> These residues can broadly be classified as surface- and interior-allosteric amino acids. Allosteric sites at the surface generally play regulatory roles that are fundamentally distinct from those within the interior; surface residues may serve as receptors or effector sites in allosteric signal transmission, whereas those within the interior may act to transmit such signals.<sup id="cite_ref-40" class="reference"><a href="#cite_note-40"><span class="cite-bracket">[</span>40<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-41" class="reference"><a href="#cite_note-41"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=24" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a href="/wiki/ASD_(database)" title="ASD (database)">ASD database</a></li> <li><a href="/wiki/Anharmonicity" title="Anharmonicity">Anharmonicity</a></li> <li><a href="/wiki/Competitive_inhibition" title="Competitive inhibition">Competitive inhibition</a></li> <li><a href="/wiki/Cooperative_binding" title="Cooperative binding">Cooperative binding</a></li> <li><a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">Enzyme kinetics</a></li> <li><a href="/wiki/Protein_dynamics" title="Protein dynamics">Protein dynamics</a></li> <li><a href="/wiki/Receptor_theory" title="Receptor theory">Receptor theory</a></li></ul> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=25" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist reflist-columns references-column-width reflist-columns-2"> <ol class="references"> <li id="cite_note-1"><span 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(May 2016). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4883016">"Identifying Allosteric Hotspots with Dynamics: Application to Inter- and Intra-species Conservation"</a>. <i>Structure</i>. <b>24</b> (5): 826–837. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.str.2016.03.008">10.1016/j.str.2016.03.008</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4883016">4883016</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/27066750">27066750</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Structure&rft.atitle=Identifying+Allosteric+Hotspots+with+Dynamics%3A+Application+to+Inter-+and+Intra-species+Conservation&rft.volume=24&rft.issue=5&rft.pages=826-837&rft.date=2016-05&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4883016%23id-name%3DPMC&rft_id=info%3Apmid%2F27066750&rft_id=info%3Adoi%2F10.1016%2Fj.str.2016.03.008&rft.aulast=Clarke&rft.aufirst=D&rft.au=Sethi%2C+A&rft.au=Li%2C+S&rft.au=Kumar%2C+S&rft.au=Chang%2C+RW&rft.au=Chen%2C+J&rft.au=Gerstein%2C+M&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4883016&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAllosteric+regulation" class="Z3988"></span></span> </li> <li id="cite_note-41"><span class="mw-cite-backlink"><b><a href="#cite_ref-41">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFDuttaEckmannLibchaberTlusty2018" class="citation journal cs1">Dutta S, Eckmann JP, Libchaber A, Tlusty T (May 2018). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5960285">"Green function of correlated genes in a minimal mechanical model of protein evolution"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. <b>115</b> (20): E4559–E4568. <a href="/wiki/ArXiv_(identifier)" class="mw-redirect" title="ArXiv (identifier)">arXiv</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://arxiv.org/abs/1801.03681">1801.03681</a></span>. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2018PNAS..115E4559D">2018PNAS..115E4559D</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1073%2Fpnas.1716215115">10.1073/pnas.1716215115</a></span>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5960285">5960285</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/29712824">29712824</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America&rft.atitle=Green+function+of+correlated+genes+in+a+minimal+mechanical+model+of+protein+evolution&rft.volume=115&rft.issue=20&rft.pages=E4559-E4568&rft.date=2018-05&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5960285%23id-name%3DPMC&rft_id=info%3Abibcode%2F2018PNAS..115E4559D&rft_id=info%3Aarxiv%2F1801.03681&rft_id=info%3Apmid%2F29712824&rft_id=info%3Adoi%2F10.1073%2Fpnas.1716215115&rft.aulast=Dutta&rft.aufirst=S&rft.au=Eckmann%2C+JP&rft.au=Libchaber%2C+A&rft.au=Tlusty%2C+T&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5960285&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAllosteric+regulation" class="Z3988"></span></span> </li> </ol></div> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Allosteric_regulation&action=edit&section=26" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1235681985">.mw-parser-output .side-box{margin:4px 0;box-sizing:border-box;border:1px solid #aaa;font-size:88%;line-height:1.25em;background-color:var(--background-color-interactive-subtle,#f8f9fa);display:flow-root}.mw-parser-output .side-box-abovebelow,.mw-parser-output .side-box-text{padding:0.25em 0.9em}.mw-parser-output .side-box-image{padding:2px 0 2px 0.9em;text-align:center}.mw-parser-output .side-box-imageright{padding:2px 0.9em 2px 0;text-align:center}@media(min-width:500px){.mw-parser-output .side-box-flex{display:flex;align-items:center}.mw-parser-output .side-box-text{flex:1;min-width:0}}@media(min-width:720px){.mw-parser-output .side-box{width:238px}.mw-parser-output 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typeof="mw:File"><span><img alt="" src="//upload.wikimedia.org/wikipedia/commons/thumb/9/99/Wiktionary-logo-en-v2.svg/40px-Wiktionary-logo-en-v2.svg.png" decoding="async" width="40" height="40" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/9/99/Wiktionary-logo-en-v2.svg/60px-Wiktionary-logo-en-v2.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/9/99/Wiktionary-logo-en-v2.svg/80px-Wiktionary-logo-en-v2.svg.png 2x" data-file-width="512" data-file-height="512" /></span></span></div> <div class="side-box-text plainlist">Look up <i><b><a href="https://en.wiktionary.org/wiki/allosteric" class="extiw" title="wiktionary:allosteric"> allosteric</a></b></i> in Wiktionary, the free dictionary.</div></div> </div> <ul><li><a rel="nofollow" class="external text" href="http://www.rsc.org/Publishing/Journals/cb/Volume/2009/3/sorting_perturbed_proteins.asp">Instant insight</a> introducing a classification system for protein allostery mechanisms from the <a 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.navbox-abovebelow{background-color:#e6e6ff}.mw-parser-output .navbox-even{background-color:#f7f7f7}.mw-parser-output .navbox-odd{background-color:transparent}.mw-parser-output .navbox .hlist td dl,.mw-parser-output .navbox .hlist td ol,.mw-parser-output .navbox .hlist td ul,.mw-parser-output .navbox td.hlist dl,.mw-parser-output .navbox td.hlist ol,.mw-parser-output .navbox td.hlist ul{padding:0.125em 0}.mw-parser-output .navbox .navbar{display:block;font-size:100%}.mw-parser-output .navbox-title .navbar{float:left;text-align:left;margin-right:0.5em}body.skin--responsive .mw-parser-output .navbox-image img{max-width:none!important}@media print{body.ns-0 .mw-parser-output .navbox{display:none!important}}</style></div><div role="navigation" class="navbox" aria-labelledby="Enzymes" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" 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navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Active_site" title="Active site">Active site</a></li> <li><a href="/wiki/Binding_site" title="Binding site">Binding site</a></li> <li><a href="/wiki/Catalytic_triad" title="Catalytic triad">Catalytic triad</a></li> <li><a href="/wiki/Oxyanion_hole" title="Oxyanion hole">Oxyanion hole</a></li> <li><a href="/wiki/Enzyme_promiscuity" title="Enzyme promiscuity">Enzyme promiscuity</a></li> <li><a href="/wiki/Diffusion-limited_enzyme" title="Diffusion-limited enzyme">Diffusion-limited enzyme</a></li> <li><a href="/wiki/Cofactor_(biochemistry)" title="Cofactor (biochemistry)">Cofactor</a></li> <li><a href="/wiki/Enzyme_catalysis" title="Enzyme catalysis">Enzyme catalysis</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Regulation</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a class="mw-selflink selflink">Allosteric regulation</a></li> <li><a href="/wiki/Cooperativity" title="Cooperativity">Cooperativity</a></li> <li><a href="/wiki/Enzyme_inhibitor" title="Enzyme inhibitor">Enzyme inhibitor</a></li> <li><a href="/wiki/Enzyme_activator" title="Enzyme activator">Enzyme activator</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Classification</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC number</a></li> <li><a href="/wiki/Protein_superfamily" title="Protein superfamily">Enzyme superfamily</a></li> <li><a href="/wiki/Protein_family" title="Protein family">Enzyme family</a></li> <li><a href="/wiki/List_of_enzymes" title="List of enzymes">List of enzymes</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Kinetics</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">Enzyme kinetics</a></li> <li><a href="/wiki/Eadie%E2%80%93Hofstee_diagram" title="Eadie–Hofstee diagram">Eadie–Hofstee diagram</a></li> <li><a href="/wiki/Hanes%E2%80%93Woolf_plot" title="Hanes–Woolf plot">Hanes–Woolf plot</a></li> <li><a href="/wiki/Lineweaver%E2%80%93Burk_plot" title="Lineweaver–Burk plot">Lineweaver–Burk plot</a></li> <li><a href="/wiki/Michaelis%E2%80%93Menten_kinetics" title="Michaelis–Menten kinetics">Michaelis–Menten kinetics</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Types</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><b>EC1 <a href="/wiki/Oxidoreductase" title="Oxidoreductase">Oxidoreductases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_1)" title="List of EC numbers (EC 1)">list</a>)</li> <li><b>EC2 <a href="/wiki/Transferase" title="Transferase">Transferases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_2)" title="List of EC numbers (EC 2)">list</a>)</li> <li><b>EC3 <a href="/wiki/Hydrolase" title="Hydrolase">Hydrolases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_3)" title="List of EC numbers (EC 3)">list</a>)</li> <li><b>EC4 <a href="/wiki/Lyase" title="Lyase">Lyases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_4)" title="List of EC numbers (EC 4)">list</a>)</li> <li><b>EC5 <a href="/wiki/Isomerase" title="Isomerase">Isomerases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_5)" title="List of EC numbers (EC 5)">list</a>)</li> <li><b>EC6 <a href="/wiki/Ligase" title="Ligase">Ligases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_6)" title="List of EC numbers (EC 6)">list</a>)</li> <li><b>EC7 <a href="/wiki/Translocase" title="Translocase">Translocases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_7)" title="List of EC numbers (EC 7)">list</a>)</li></ul> </div></td></tr></tbody></table></div>    </div><noscript><img src="https://login.wikimedia.org/wiki/Special:CentralAutoLogin/start?type=1x1" alt="" width="1" height="1" style="border: none; position: absolute;"></noscript> <div class="printfooter" data-nosnippet="">Retrieved from "<a dir="ltr" href="https://en.wikipedia.org/w/index.php?title=Allosteric_regulation&oldid=1248376656">https://en.wikipedia.org/w/index.php?title=Allosteric_regulation&oldid=1248376656</a>"</div></div> <div id="catlinks" class="catlinks" data-mw="interface"><div id="mw-normal-catlinks" class="mw-normal-catlinks"><a href="/wiki/Help:Category" title="Help:Category">Categories</a>: <ul><li><a href="/wiki/Category:Proteins" title="Category:Proteins">Proteins</a></li><li><a href="/wiki/Category:Enzyme_kinetics" title="Category:Enzyme kinetics">Enzyme kinetics</a></li></ul></div><div id="mw-hidden-catlinks" 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