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style="text-align:center;font-size:125%;font-weight:bold">interstitial collagenase</th></tr><tr><td colspan="4" style="text-align:center"></td></tr><tr><th colspan="4" style="text-align:center;background-color:#ddd">Identifiers</th></tr><tr><th scope="row" style="background-color:#c3fdb8"><span class="plainlinks"><a href="/wiki/Gene_nomenclature" title="Gene nomenclature">Aliases</a></span></th><td colspan="3" style="background:#eee"><span class="plainlinks"></span></td></tr><tr><th scope="row" style="background-color:#c3fdb8">External IDs</th><td colspan="3" style="background-color:#eee"><span class="plainlinks"><a href="/wiki/GeneCards" title="GeneCards">GeneCards</a>: <a rel="nofollow" class="external autonumber" href="https://www.genecards.org/cgi-bin/carddisp.pl?gene=">[1]</a>; <a href="/wiki/Orthologous_MAtrix" title="Orthologous MAtrix">OMA</a>:<a rel="nofollow" class="external text" href="https://omabrowser.org/oma/vps/n/a">- orthologs</a></span></td></tr><tr><td colspan="4" style="text-align:center;background-color:#eee"><table class="collapsible" style="padding:0;border:none;margin:0;width:100%;text-align:left"><tbody><tr><th colspan="4" style="text-align:center;background-color:#ddd"><a href="/wiki/Orthologs" class="mw-redirect" title="Orthologs">Orthologs</a></th></tr><tr><th scope="row" style="background-color:#c3fdb8">Species</th><td><b>Human</b></td><td><b>Mouse</b></td></tr><tr><th scope="row" style="background-color:#c3fdb8"><a href="/wiki/Entrez" title="Entrez">Entrez</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"><span class="plainlinks"></span></th></tr><tr><td colspan="1"><p class="plainlinks">n/a</p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"><span class="plainlinks"></span></th></tr><tr><td colspan="1"><p class="plainlinks">n/a</p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:#c3fdb8"><a href="/wiki/Ensembl" class="mw-redirect" title="Ensembl">Ensembl</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"><span class="plainlinks"></span></th></tr><tr><td colspan="1"><p class="plainlinks">n/a</p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"><span class="plainlinks"></span></th></tr><tr><td colspan="1"><p class="plainlinks">n/a</p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:#c3fdb8"><a href="/wiki/UniProt" title="UniProt">UniProt</a></th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"><span class="plainlinks"></span></th></tr><tr><td colspan="1"><p class="plainlinks"><a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprot/n">n</a><br /><a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprot/a">a</a></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1"><span class="plainlinks"></span></th></tr><tr><td colspan="1"><p class="plainlinks">n/a</p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:#c3fdb8">RefSeq (mRNA)</th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1" class="plainlinks"></th></tr><tr><td colspan="1"><p><span class="plainlinks">n/a</span></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1" class="plainlinks"></th></tr><tr><td colspan="1"><p><span class="plainlinks">n/a</span></p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:#c3fdb8">RefSeq (protein)</th><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1" class="plainlinks"></th></tr><tr><td colspan="1"><p><span class="plainlinks">n/a</span></p></td></tr></tbody></table></td><td><table class="none" style="padding:0;border:none;margin:0;width:100%;text-align:right"><tbody><tr><th colspan="1" class="plainlinks"></th></tr><tr><td colspan="1"><p><span class="plainlinks">n/a</span></p></td></tr></tbody></table></td></tr><tr><th scope="row" style="background-color:#c3fdb8">Location (UCSC)</th><td><span class="plainlinks">n/a</span></td><td><span class="plainlinks">n/a</span></td></tr><tr><th scope="row" style="background-color:#c3fdb8"><a href="/wiki/PubMed" title="PubMed">PubMed</a> search</th><td><span class="plainlinks">n/a</span></td><td><span class="plainlinks">n/a</span></td></tr></tbody></table></td></tr><tr><td colspan="4" style="text-align:center;background-color:#eee"><a href="/wiki/Wikidata" title="Wikidata">Wikidata</a></td></tr><tr><td colspan="4" style="text-align:center;background-color:#eee"><table style="padding:0;border:none;margin:0;width:100%;text-align:center"><tbody><tr><td colspan="4" style="background-color:#eee;text-align:center"><a href="https://www.wikidata.org/wiki/Q13033710" class="extiw" title="d:Q13033710">View/Edit Human</a></td><td colspan="0" style="background-color:#eee;text-align:center"></td></tr></tbody></table></td></tr></tbody></table> <p><b>Interstitial collagenase</b>, also known as <b>fibroblast collagenase</b> and <b>matrix metalloproteinase-1</b> (<b>MMP-1</b>), is an <a href="/wiki/Enzyme" title="Enzyme">enzyme</a> that in humans is encoded by the <i>MMP1</i> <a href="/wiki/Gene" title="Gene">gene</a>.<sup id="cite_ref-UniProt_1-0" class="reference"><a href="#cite_note-UniProt-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-entrez_2-0" class="reference"><a href="#cite_note-entrez-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid3027129_3-0" class="reference"><a href="#cite_note-pmid3027129-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid8921407_4-0" class="reference"><a href="#cite_note-pmid8921407-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> The gene is part of a cluster of MMP genes which localize to <a href="/wiki/11q" class="mw-redirect" title="11q">chromosome 11q22.3.</a><sup id="cite_ref-entrez_2-1" class="reference"><a href="#cite_note-entrez-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> MMP-1 was the first vertebrate <a href="/wiki/Collagenase" title="Collagenase">collagenase</a> both purified to homogeneity as a protein, and cloned as a <a href="/wiki/Complementary_DNA" title="Complementary DNA">cDNA</a>.<sup id="cite_ref-pmid13902219_5-0" class="reference"><a href="#cite_note-pmid13902219-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid3009463_6-0" class="reference"><a href="#cite_note-pmid3009463-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> MMP-1 has an estimated <a href="/wiki/Molecular_mass" title="Molecular mass">molecular mass</a> of 54 kDa.<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> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Structure">Structure</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Interstitial_collagenase&action=edit&section=1" title="Edit section: Structure"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>MMP-1 has an archetypal structure consisting of a pre-domain, a pro-domain, a <a href="/wiki/Catalytic_domain" class="mw-redirect" title="Catalytic domain">catalytic domain</a>, a linker region and a <a href="/wiki/Hemopexin" title="Hemopexin">hemopexin</a>-like domain.<sup id="cite_ref-pmid8590015_8-0" class="reference"><a href="#cite_note-pmid8590015-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> The primary structure of MMP-1 was first published by Goldberg, G I, <i>et al.</i><sup id="cite_ref-pmid3009463_6-1" class="reference"><a href="#cite_note-pmid3009463-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> Two main nomenclatures for the primary structure are currently in use, the original one from which the first amino-acid starts with the signalling peptide and a second one where the first amino-acid starts counting from the prodomain (proenzyme nomenclature). </p> <div class="mw-heading mw-heading3"><h3 id="Catalytic_domain">Catalytic domain</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Interstitial_collagenase&action=edit&section=2" title="Edit section: Catalytic domain"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The catalytic domains of MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40 Å.<sup id="cite_ref-pmid19374923_9-0" class="reference"><a href="#cite_note-pmid19374923-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> Despite the similarity of the catalytic domains of MMPs, this entry will focus only on the structural features of MMP-1 catalytic domain. </p> <div class="mw-heading mw-heading4"><h4 id="Overall_structural_characteristics">Overall structural characteristics</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Interstitial_collagenase&action=edit&section=3" title="Edit section: Overall structural characteristics"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/Catalytic_domain" class="mw-redirect" title="Catalytic domain">catalytic domain</a> of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca<sup>2+</sup> and two Zn<sup>2+</sup>, one of which with catalytic role.<sup id="cite_ref-pmid8090713_10-0" class="reference"><a href="#cite_note-pmid8090713-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> </p><p>The catalytic domain (CAT) of MMP-1 starts with the F100 (non-truncated CAT) as the first amino-acid of the N-terminal loop of the CAT domain. The first published x-ray structure of the CAT domain was representative of the truncated form of this domain, where the first 7 amino-acids are not present.<sup id="cite_ref-pmid8090713_10-1" class="reference"><a href="#cite_note-pmid8090713-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> </p><p>After the initial loop, the sequences follows to the first and longest β-sheet (sI). A second loop precedes large "amphipathic α-helix" (hA) that longitudinally spans protein site. The β-strands sII and sIII follows separated by the respective loops, loop 4 being commonly designated as "short loop" bridging sII to sIII. Following the sIII strand the sequence meets the 'S-shaped double loop' that is of primary importance for the peptide structure and catalytic activity (see further) as it extends to the cleft side "bulge", continuing to the only antiparallel β-strand sIV, which is prime importance for binding peptidic substrates or inhibitors by forming main chain <a href="/wiki/Hydrogen_bonds" class="mw-redirect" title="Hydrogen bonds">hydrogen bond</a>. Following sIV, loop Gln186-Gly192 and β-strand sV are responsible for contributing with many ligands to the several metal ions present in the protein (read further). A large open loop follows sV which has proven importance in substrate specificity within the MMPs family.<sup id="cite_ref-pmid14668538_11-0" class="reference"><a href="#cite_note-pmid14668538-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> A specific region (183)RWTNNFREY(191) has been identified as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity.<sup id="cite_ref-pmid10871619_12-0" class="reference"><a href="#cite_note-pmid10871619-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> On C-terminal part of the CAT Domain the hB α-helix, known as the "active-site helix" encompasses part of the "zinc-binding consensus sequence" HEXXHXXGXXH that is characteristic of the <a href="/w/index.php?title=Metzincin_superfamily&action=edit&redlink=1" class="new" title="Metzincin superfamily (page does not exist)">Metzincin superfamily</a>.<sup id="cite_ref-pmid8405391_13-0" class="reference"><a href="#cite_note-pmid8405391-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid7663339_14-0" class="reference"><a href="#cite_note-pmid7663339-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> The α-helix hB finishes abruptly at Gly225 where the last loop of the domain starts. This last loop contains the "specificity loop" which is the shortest in the MMPs family. The Catalytic Domain ends at Gly261 with α-helix hC. </p> <div class="mw-heading mw-heading2"><h2 id="Function">Function</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Interstitial_collagenase&action=edit&section=4" title="Edit section: Function"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Matrix_metalloproteinase" title="Matrix metalloproteinase">MMPs</a> are involved in the breakdown of <a href="/wiki/Extracellular_matrix" title="Extracellular matrix">extracellular matrix</a> in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Specifically, MMP-1 breaks down the interstitial <a href="/wiki/Collagen" title="Collagen">collagens</a>, types I, II, and III. </p> <table> <tbody><tr> <td><figure class="mw-halign-left" typeof="mw:File/Thumb"><a href="/wiki/File:Matrix_metalloproteinase_in_rat_cornea_after_artificial_tears_Ciprofloxacin_Ofloxacin_Levofloxacin.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/4/49/Matrix_metalloproteinase_in_rat_cornea_after_artificial_tears_Ciprofloxacin_Ofloxacin_Levofloxacin.jpg/240px-Matrix_metalloproteinase_in_rat_cornea_after_artificial_tears_Ciprofloxacin_Ofloxacin_Levofloxacin.jpg" decoding="async" width="240" height="160" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/4/49/Matrix_metalloproteinase_in_rat_cornea_after_artificial_tears_Ciprofloxacin_Ofloxacin_Levofloxacin.jpg/360px-Matrix_metalloproteinase_in_rat_cornea_after_artificial_tears_Ciprofloxacin_Ofloxacin_Levofloxacin.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/4/49/Matrix_metalloproteinase_in_rat_cornea_after_artificial_tears_Ciprofloxacin_Ofloxacin_Levofloxacin.jpg/480px-Matrix_metalloproteinase_in_rat_cornea_after_artificial_tears_Ciprofloxacin_Ofloxacin_Levofloxacin.jpg 2x" data-file-width="1200" data-file-height="801" /></a><figcaption>Induction of matrix metalloproteinase 1 in <a href="/wiki/Rat" title="Rat">rat</a> corneas by <a href="/wiki/Ciprofloxacin" title="Ciprofloxacin">ciprofloxacin</a>, <a href="/wiki/Ofloxacin" title="Ofloxacin">ofloxacin</a> and <a href="/wiki/Levofloxacin" title="Levofloxacin">levofloxacin</a> (b,c,d) compared to <a href="/wiki/Artificial_tear" class="mw-redirect" title="Artificial tear">artificial tears</a> (a). Reviglio et al., 2003.</figcaption></figure> </td></tr></tbody></table> <div class="mw-heading mw-heading2"><h2 id="Regulation">Regulation</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Interstitial_collagenase&action=edit&section=5" title="Edit section: Regulation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Mechanical force may increase the expression of MMP1 in human periodontal ligament cells.<sup id="cite_ref-pmid18705799_15-0" class="reference"><a href="#cite_note-pmid18705799-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup> During cancer progression, MMP1 can be dysregulated by different mechanisms, including the activation of an <a href="/wiki/Insulator_(genetics)" title="Insulator (genetics)">insulator element</a> located between <a href="/wiki/MMP8" title="MMP8">MMP8</a> and <a href="/wiki/MMP10" title="MMP10">MMP10</a> genes.<sup id="cite_ref-pmid38017545_16-0" class="reference"><a href="#cite_note-pmid38017545-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Interactions">Interactions</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Interstitial_collagenase&action=edit&section=6" title="Edit section: Interactions"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>MMP1 has been shown to <a href="/wiki/Protein-protein_interaction" class="mw-redirect" title="Protein-protein interaction">interact</a> with <a href="/wiki/CD49b" class="mw-redirect" title="CD49b">CD49b</a>.<sup id="cite_ref-pmid11359774_17-0" class="reference"><a href="#cite_note-pmid11359774-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid11359786_18-0" class="reference"><a href="#cite_note-pmid11359786-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> </p> <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=Interstitial_collagenase&action=edit&section=7" 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" style="column-width: 35em;"> <ol class="references"> <li id="cite_note-UniProt-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-UniProt_1-0">^</a></b></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free 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"Is collagenase (matrix metalloproteinase-1) necessary for bone and other connective tissue remodeling?". <i>Clin. Orthop. Relat. Res.</i> (313): 47–53. <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/7641497">7641497</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Clin.+Orthop.+Relat.+Res.&rft.atitle=Is+collagenase+%28matrix+metalloproteinase-1%29+necessary+for+bone+and+other+connective+tissue+remodeling%3F&rft.issue=313&rft.pages=47-53&rft.date=1995&rft_id=info%3Apmid%2F7641497&rft.aulast=Krane&rft.aufirst=SM&rfr_id=info%3Asid%2Fen.wikipedia.org%3AInterstitial+collagenase" class="Z3988"></span></li> <li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFMassovaKotraFridmanMobashery1998" class="citation journal cs1">Massova I, Kotra LP, Fridman R, Mobashery S (1998). 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class="Z3988"></span></li> <li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFGolubkovStrongin2007" class="citation journal cs1">Golubkov VS, Strongin AY (2007). <a rel="nofollow" class="external text" href="https://doi.org/10.4161%2Fcc.6.2.3706">"Proteolysis-driven oncogenesis"</a>. <i>Cell Cycle</i>. <b>6</b> (2): 147–50. <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/10.4161%2Fcc.6.2.3706">10.4161/cc.6.2.3706</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/17245132">17245132</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Cell+Cycle&rft.atitle=Proteolysis-driven+oncogenesis&rft.volume=6&rft.issue=2&rft.pages=147-50&rft.date=2007&rft_id=info%3Adoi%2F10.4161%2Fcc.6.2.3706&rft_id=info%3Apmid%2F17245132&rft.aulast=Golubkov&rft.aufirst=VS&rft.au=Strongin%2C+AY&rft_id=https%3A%2F%2Fdoi.org%2F10.4161%252Fcc.6.2.3706&rfr_id=info%3Asid%2Fen.wikipedia.org%3AInterstitial+collagenase" class="Z3988"></span></li></ul> </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=Interstitial_collagenase&action=edit&section=9" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li>The <a href="/wiki/MEROPS" title="MEROPS">MEROPS</a> online database for peptidases and their inhibitors: <a rel="nofollow" class="external text" href="http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M10.001">M10.001</a></li> <li>Overview of all the structural information available in the <a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a> for <a href="/wiki/UniProt" title="UniProt">UniProt</a>: <i><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P03956">P03956</a></i> (Interstitial collagenase) at the <a href="/wiki/PDBe-KB" title="PDBe-KB">PDBe-KB</a>.</li></ul> <p><br /> </p> <div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist li{margin:0;display:inline}.mw-parser-output .hlist.inline,.mw-parser-output .hlist.inline dl,.mw-parser-output .hlist.inline ol,.mw-parser-output .hlist.inline ul,.mw-parser-output .hlist dl dl,.mw-parser-output .hlist dl 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srcset="//upload.wikimedia.org/wikipedia/commons/thumb/1/12/PDB_2clt_EBI.jpg/270px-PDB_2clt_EBI.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/1/12/PDB_2clt_EBI.jpg/360px-PDB_2clt_EBI.jpg 2x" data-file-width="800" data-file-height="600" /></a></span></div> <div class="gallerytext"><b>2clt</b>: CRYSTAL STRUCTURE OF THE ACTIVE FORM (FULL-LENGTH) OF HUMAN FIBROBLAST COLLAGENASE.</div> </li> <li class="gallerybox" style="width: 215px"> <div class="thumb" style="width: 210px; height: 210px;"><span typeof="mw:File"><a href="/wiki/File:PDB_2j0t_EBI.jpg" class="mw-file-description" title="2j0t: CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP-1 IN COMPLEX WITH THE INHIBITORY DOMAIN OF TIMP-1"><img alt="2j0t: CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP-1 IN COMPLEX WITH THE INHIBITORY DOMAIN OF TIMP-1" src="//upload.wikimedia.org/wikipedia/commons/thumb/5/57/PDB_2j0t_EBI.jpg/180px-PDB_2j0t_EBI.jpg" decoding="async" width="180" height="135" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/5/57/PDB_2j0t_EBI.jpg/270px-PDB_2j0t_EBI.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/5/57/PDB_2j0t_EBI.jpg/360px-PDB_2j0t_EBI.jpg 2x" data-file-width="800" data-file-height="600" /></a></span></div> <div class="gallerytext"><b>2j0t</b>: CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP-1 IN COMPLEX WITH THE INHIBITORY DOMAIN OF TIMP-1</div> </li> <li class="gallerybox" style="width: 215px"> <div class="thumb" style="width: 210px; height: 210px;"><span typeof="mw:File"><a href="/wiki/File:PDB_2tcl_EBI.jpg" class="mw-file-description" title="2tcl: STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR"><img alt="2tcl: STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR" src="//upload.wikimedia.org/wikipedia/commons/thumb/3/38/PDB_2tcl_EBI.jpg/180px-PDB_2tcl_EBI.jpg" decoding="async" width="180" height="135" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/3/38/PDB_2tcl_EBI.jpg/270px-PDB_2tcl_EBI.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/3/38/PDB_2tcl_EBI.jpg/360px-PDB_2tcl_EBI.jpg 2x" data-file-width="800" data-file-height="600" /></a></span></div> <div class="gallerytext"><b>2tcl</b>: STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR</div> </li> <li class="gallerybox" style="width: 215px"> <div class="thumb" style="width: 210px; height: 210px;"><span typeof="mw:File"><a href="/wiki/File:PDB_3ayk_EBI.jpg" class="mw-file-description" title="3ayk: CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, MINIMIZED AVERAGE STRUCTURE"><img alt="3ayk: CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, MINIMIZED AVERAGE STRUCTURE" src="//upload.wikimedia.org/wikipedia/commons/thumb/2/26/PDB_3ayk_EBI.jpg/180px-PDB_3ayk_EBI.jpg" decoding="async" width="180" height="135" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/2/26/PDB_3ayk_EBI.jpg/270px-PDB_3ayk_EBI.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/2/26/PDB_3ayk_EBI.jpg/360px-PDB_3ayk_EBI.jpg 2x" data-file-width="800" data-file-height="600" /></a></span></div> <div class="gallerytext"><b>3ayk</b>: CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, MINIMIZED AVERAGE STRUCTURE</div> </li> <li class="gallerybox" style="width: 215px"> <div class="thumb" style="width: 210px; height: 210px;"><span typeof="mw:File"><a href="/wiki/File:PDB_4ayk_EBI.jpg" class="mw-file-description" title="4ayk: CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, 30 STRUCTURES"><img alt="4ayk: CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, 30 STRUCTURES" src="//upload.wikimedia.org/wikipedia/commons/thumb/d/d8/PDB_4ayk_EBI.jpg/180px-PDB_4ayk_EBI.jpg" decoding="async" width="180" height="135" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/d/d8/PDB_4ayk_EBI.jpg/270px-PDB_4ayk_EBI.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/d/d8/PDB_4ayk_EBI.jpg/360px-PDB_4ayk_EBI.jpg 2x" data-file-width="800" data-file-height="600" /></a></span></div> <div class="gallerytext"><b>4ayk</b>: CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, 30 STRUCTURES</div> </li> <li class="gallerybox" style="width: 215px"> <div class="thumb" style="width: 210px; height: 210px;"><span typeof="mw:File"><a href="/wiki/File:PDB_966c_EBI.jpg" class="mw-file-description" title="966c: CRYSTAL STRUCTURE OF FIBROBLAST COLLAGENASE-1 COMPLEXED TO A DIPHENYL-ETHER SULPHONE BASED HYDROXAMIC ACID"><img alt="966c: CRYSTAL STRUCTURE OF FIBROBLAST COLLAGENASE-1 COMPLEXED TO A DIPHENYL-ETHER SULPHONE BASED HYDROXAMIC ACID" src="//upload.wikimedia.org/wikipedia/commons/thumb/b/bb/PDB_966c_EBI.jpg/180px-PDB_966c_EBI.jpg" decoding="async" width="180" height="135" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/b/bb/PDB_966c_EBI.jpg/270px-PDB_966c_EBI.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/b/bb/PDB_966c_EBI.jpg/360px-PDB_966c_EBI.jpg 2x" data-file-width="800" data-file-height="600" /></a></span></div> <div class="gallerytext"><b>966c</b>: CRYSTAL STRUCTURE OF FIBROBLAST COLLAGENASE-1 COMPLEXED TO A DIPHENYL-ETHER SULPHONE BASED HYDROXAMIC ACID</div> </li> </ul></div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235"></div><div role="navigation" class="navbox" aria-labelledby="Proteases:_metalloendopeptidases_(EC_3.4.24)" 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" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231"><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Metalloendopeptidases" title="Template:Metalloendopeptidases"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Metalloendopeptidases" title="Template talk:Metalloendopeptidases"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Metalloendopeptidases" title="Special:EditPage/Template:Metalloendopeptidases"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Proteases:_metalloendopeptidases_(EC_3.4.24)" style="font-size:114%;margin:0 4em"><a href="/wiki/Protease" title="Protease">Proteases</a>: <a href="/wiki/Metalloendopeptidase" title="Metalloendopeptidase">metalloendopeptidases</a> (<a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC</a> <a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.24:_Metallopeptidases" title="List of EC numbers (EC 3)">3.4.24</a>)</div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/A_disintegrin_and_metalloproteinase" class="mw-redirect" title="A disintegrin and metalloproteinase">ADAM proteins</a></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/Alpha_secretase" title="Alpha secretase">Alpha secretases</a> <ul><li><a href="/wiki/ADAM9" title="ADAM9">ADAM9</a></li> <li><a href="/wiki/ADAM10" title="ADAM10">ADAM10</a></li> <li><a href="/wiki/ADAM17" title="ADAM17">ADAM17</a></li> <li><a href="/wiki/ADAM19" title="ADAM19">ADAM19</a></li></ul></li> <li><a href="/wiki/ADAM2" title="ADAM2">ADAM2</a></li> <li><a href="/wiki/ADAM7" title="ADAM7">ADAM7</a></li> <li><a href="/wiki/ADAM8" title="ADAM8">ADAM8</a></li> <li><a href="/wiki/ADAM11" title="ADAM11">ADAM11</a></li> <li><a href="/wiki/ADAM12" title="ADAM12">ADAM12</a></li> <li><a href="/wiki/ADAM15" title="ADAM15">ADAM15</a></li> <li><a href="/wiki/ADAM18" title="ADAM18">ADAM18</a></li> <li><a href="/wiki/ADAM22" title="ADAM22">ADAM22</a></li> <li><a href="/wiki/ADAM23" title="ADAM23">ADAM23</a></li> <li><a href="/wiki/ADAM28" title="ADAM28">ADAM28</a></li> <li><a href="/wiki/ADAM33" title="ADAM33">ADAM33</a></li> <li><a href="/wiki/ADAMTS1" title="ADAMTS1">ADAMTS1</a></li> <li><a href="/wiki/ADAMTS2" title="ADAMTS2">ADAMTS2</a></li> <li><a href="/wiki/ADAMTS3" title="ADAMTS3">ADAMTS3</a></li> <li><a href="/wiki/ADAMTS4" title="ADAMTS4">ADAMTS4</a></li> <li><a href="/wiki/ADAMTS5" title="ADAMTS5">ADAMTS5</a></li> <li><a href="/wiki/ADAMTS8" title="ADAMTS8">ADAMTS8</a></li> <li><a href="/wiki/ADAMTS9" title="ADAMTS9">ADAMTS9</a></li> <li><a href="/wiki/ADAMTS10" title="ADAMTS10">ADAMTS10</a></li> <li><a href="/wiki/ADAMTS12" title="ADAMTS12">ADAMTS12</a></li> <li><a href="/wiki/ADAMTS13" title="ADAMTS13">ADAMTS13</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Matrix_metalloproteinase" title="Matrix metalloproteinase">Matrix metalloproteinases</a></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/Collagenase" title="Collagenase">Collagenases</a> <ul><li><a href="/wiki/MMP1" class="mw-redirect" title="MMP1">MMP1</a></li> <li><a href="/wiki/MMP8" title="MMP8">MMP8</a></li></ul></li> <li><a href="/wiki/Gelatinase" title="Gelatinase">Gelatinases</a> <ul><li><a href="/wiki/MMP2" title="MMP2">MMP2</a></li> <li><a href="/wiki/MMP9" title="MMP9">MMP9</a></li></ul></li> <li><a href="/wiki/MMP3" title="MMP3">MMP3</a></li> <li><a href="/wiki/MMP7" title="MMP7">MMP7</a></li> <li><a href="/wiki/MMP10" title="MMP10">MMP10</a></li> <li><a href="/wiki/MMP11" title="MMP11">MMP11</a></li> <li><a href="/wiki/Matrix_metallopeptidase_12" title="Matrix metallopeptidase 12">MMP12</a></li> <li><a href="/wiki/Matrix_metallopeptidase_13" title="Matrix metallopeptidase 13">MMP13</a></li> <li><a href="/wiki/MMP14" title="MMP14">MMP14</a></li> <li><a href="/wiki/MMP15" title="MMP15">MMP15</a></li> <li><a href="/wiki/MMP16" title="MMP16">MMP16</a></li> <li><a href="/wiki/MMP17" title="MMP17">MMP17</a></li> <li><a href="/wiki/MMP19" title="MMP19">MMP19</a></li> <li><a href="/wiki/MMP20" title="MMP20">MMP20</a></li> <li><a href="/wiki/MMP21" title="MMP21">MMP21</a></li> <li><a href="/w/index.php?title=MMP23A&action=edit&redlink=1" class="new" title="MMP23A (page does not exist)">MMP23A</a></li> <li><a href="/wiki/MMP23B" title="MMP23B">MMP23B</a></li> <li><a href="/wiki/MMP24" title="MMP24">MMP24</a></li> <li><a href="/wiki/MMP25" title="MMP25">MMP25</a></li> <li><a href="/wiki/MMP26" title="MMP26">MMP26</a></li> <li><a href="/wiki/MMP27" title="MMP27">MMP27</a></li> <li><a href="/wiki/MMP28" title="MMP28">MMP28</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other</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/Neprilysin" title="Neprilysin">Neprilysin</a></li> <li><a href="/wiki/Procollagen_peptidase" title="Procollagen peptidase">Procollagen peptidase</a></li> <li><a href="/wiki/Thermolysin" title="Thermolysin">Thermolysin</a></li> <li><a href="/wiki/Pregnancy-associated_plasma_protein_A" class="mw-redirect" title="Pregnancy-associated plasma protein A">Pregnancy-associated plasma protein A</a></li> <li><a href="/wiki/Bone_morphogenetic_protein_1" title="Bone morphogenetic protein 1">Bone morphogenetic protein 1</a></li> <li><a href="/wiki/Lysostaphin" title="Lysostaphin">Lysostaphin</a></li> <li><a href="/wiki/Insulin-degrading_enzyme" title="Insulin-degrading enzyme">Insulin-degrading enzyme</a></li> <li><a href="/wiki/ZMPSTE24" title="ZMPSTE24">ZMPSTE24</a></li></ul> </div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235"></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" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231"><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Enzymes" title="Template:Enzymes"><abbr title="View 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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 href="/wiki/Allosteric_regulation" title="Allosteric regulation">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> <style data-mw-deduplicate="TemplateStyles:r1130092004">.mw-parser-output .portal-bar{font-size:88%;font-weight:bold;display:flex;justify-content:center;align-items:baseline}.mw-parser-output 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