5fpe: Difference between revisions
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<StructureSection load='5fpe' size='340' side='right'caption='[[5fpe]], [[Resolution|resolution]] 1.96Å' scene=''> | <StructureSection load='5fpe' size='340' side='right'caption='[[5fpe]], [[Resolution|resolution]] 1.96Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5fpe]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5fpe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FPE FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3TR:3-AMINO-1,2,4-TRIAZOLE'>3TR</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fpe OCA], [https://pdbe.org/5fpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fpe RCSB], [https://www.ebi.ac.uk/pdbsum/5fpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fpe ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HSP72_HUMAN HSP72_HUMAN] In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Jhoti | [[Category: Jhoti H]] | ||
[[Category: Ludlow | [[Category: Ludlow RF]] | ||
[[Category: Patel | [[Category: Patel S]] | ||
[[Category: Saini | [[Category: Saini HK]] | ||
[[Category: Tickle | [[Category: Tickle IJ]] | ||
[[Category: Verdonk | [[Category: Verdonk M]] | ||