4fsv
From Proteopedia
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==Crystal structure of a heat shock 70kDa protein 2 (HSPA2) from Homo sapiens at 1.80 A resolution== | ==Crystal structure of a heat shock 70kDa protein 2 (HSPA2) from Homo sapiens at 1.80 A resolution== | ||
- | <StructureSection load='4fsv' size='340' side='right' caption='[[4fsv]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4fsv' size='340' side='right'caption='[[4fsv]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4fsv]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4fsv]] is a 1 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=4FSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FSV FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
- | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fsv OCA], [https://pdbe.org/4fsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fsv RCSB], [https://www.ebi.ac.uk/pdbsum/4fsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fsv ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</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. |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
- | [[Category: | + | [[Category: Large Structures]] |
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Revision as of 20:09, 19 October 2022
Crystal structure of a heat shock 70kDa protein 2 (HSPA2) from Homo sapiens at 1.80 A resolution
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