PDB-101: Geis Archive: DPG-Hemoglobin Complex

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var jsmolLoaded = false; function loadIframe() { if (jsmolLoaded == false) { var src = '/sci-art/geis-archive/jsmol/geis-0299-dpg-bound-hemoglobin'; $("#jsmol-iframe").attr('src', src); jsmolLoaded = true; } } </script> <div id="sub-navbar"> <div class="row hidden-print"> <div class="col-xs-12 col-sm-6 sub-navbar"> <h4>Geis Digital Archive</h4> </div> <div class="col-xs-12 col-sm-6 text-right sub-navbar"> <table> <tr> <td onclick="location.href="/sci-art/geis-archive/about"">About</td> <td onclick="location.href="/sci-art/geis-archive/gallery-by-date"">Gallery by Date</td> <td onclick="location.href="/sci-art/geis-archive/gallery-by-name"">Gallery by Name</td> <td onclick="location.href="/sci-art/geis-archive/irving-geis"">Irving Geis</td> </tr> </table> </div> </div> </div> <div data-elastic-include> <div class="row"> <div class="col-md-7 col-md-push-5 col-sm-12"> <div class="row"> <div class="col-xs-8"> <h1>DPG-Hemoglobin Complex</h1> <p>Unknown Year, Unknown Dimensions</p> </div> <div class="col-xs-4"><img src="https://cdn.rcsb.org/pdb101/geis/images/logos/geis-0299.png" class="img-responsive geis-logo"> </div> </div> <p><p>Geis illustrates the complex of DPG (2,3-diphosphoglycerate) with hemoglobin as a co-crystal. The charged amino acid residues stabilizing the complex with DPG are drawn in blue.</p></p> <p><small><i>Used with permission from the Howard Hughes Medical Institute (<a href='http://www.hhmi.org', target='_blank'>www.hhmi.org</a>). All rights reserved.</i></small></p> <p><a href="/sci-art/geis-archive/reprint-request/geis-0299-dpg-bound-hemoglobin" class="btn btn-primary">Non-commercial Reprint Request</a></p> </div> <div style="margin-top:20px;" class="col-md-5 col-md-pull-7 col-sm-12"><a href="https://cdn.rcsb.org/pdb101/geis/images/1000w/geis-0299-dpg-bound-hemoglobin.png" data-toggle="lightbox" data-title="DPG-Hemoglobin Complex" data-footer="<i>Used with permission from the Howard Hughes Medical Institute (<a href="http://www.hhmi.org", target="_blank">www.hhmi.org</a>). All rights reserved.</i>"><img src="https://cdn.rcsb.org/pdb101/geis/images/600/geis-0299-dpg-bound-hemoglobin.png" class="img-responsive border"></a> </div> </div> <hr> <div class="row"> <div class="col-lg-5 col-sm-12"> <div id="media-tabs"> <ul class="nav nav-tabs"> <li class="active"><a data-toggle="tab" href="#tabs-image">Image</a></li> <li><a data-toggle="tab" href="#tabs-jsmol" onclick="loadIframe();">3D Interactive</a></li> <li><a data-toggle="tab" href="#tabs-video">Video</a></li> </ul> <div class="tab-content"> <div id="tabs-image" class="tab-pane active"><img src="https://cdn.rcsb.org/pdb101/geis/images/static/geis-0299-dpg-bound-hemoglobin.png" class="img-responsive"></div> <div id="tabs-jsmol" class="tab-pane"> <iframe id="jsmol-iframe" marginheight="0" marginwidth="0" scrolling="no" frameborder="0"></iframe> </div> <div id="tabs-video" class="tab-pane"> <video controls="yes" loop="yes" width="100%"> <source src="https://cdn.rcsb.org/pdb101/geis/mp4/geis-0299-dpg-bound-hemoglobin.mp4" type="video/mp4"> </video> </div> </div> </div> <p>Related PDB Entry: <a href='http://www.rcsb.org/pdb/explore/explore.do?structureId=4L7Y' target='_blank'>4L7Y</a></p> <h6>Experimental Structure Citation</h6> <p>To be published. Authors: Safo, M.K., Chowdhury, N.</p> </div> <div class="col-lg-7 col-sm-12"> <h2>About DPG-Hemoglobin Complex</h2> <p><p> 2,3-diphosphoglycerate (DPG) is an inorganic phosphate produced in red cells. When DPG binds to deoxyhemoglobin, it acts to stabilize the low oxygen affinity state (T state) of the oxygen carrier. It fits neatly into the cavity of the deoxy- conformation, forming salt bridges with lysine and histidine residues in the ß subunits of hemoglobin. The R state, with oxygen bound to a heme group, has a different conformation and does not allow this interaction. By itself, hemoglobin has sigmoid-like kinetics, which makes easier another subunits’ binding.</p> <p><b>Text Refrences</b></p> <p>Reinhold Benesch, Ruth E. Benesch. (1967). The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin. Biochem Biophys Res Commun. 26(2):162–167. </p></p> </div> </div> </div> </div> <div id="footer_main" class="hidden-print"> <div class="container"> <div class="row"> <div class="col-sm-12 col-md-7"> <p><strong>About PDB-101</strong></p> <p>Researchers around the globe make 3D structures freely available from the Protein Data Bank (PDB) archive. PDB-101 training materials help graduate students, postdoctoral scholars, and researchers use PDB data and RCSB PDB tools. Outreach content demonstrate how PDB data impact fundamental biology, biomedicine, bioengineering/biotechnology, and energy sciences in 3D for a diverse and multidisciplinary user community. 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PDB-101: Geis Archive: DPG-Hemoglobin Complex