7gyg
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of HSP72 in complex with ligand 10 at 14.82 MGy X-ray dose.== | |
| - | + | <StructureSection load='7gyg' size='340' side='right'caption='[[7gyg]], [[Resolution|resolution]] 1.92Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[7gyg]] 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=7GYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7GYG FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GBA:(2~{R},3~{R},4~{S},5~{R})-2-(6-azanyl-8-bromanyl-purin-9-yl)-5-(hydroxymethyl)oxolane-3,4-diol'>GBA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7gyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7gyg OCA], [https://pdbe.org/7gyg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7gyg RCSB], [https://www.ebi.ac.uk/pdbsum/7gyg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7gyg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HS71A_HUMAN HS71A_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. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).<ref>PMID:16537599</ref> <ref>PMID:22528486</ref> <ref>PMID:23973223</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cabry M]] | ||
| + | [[Category: Le Bihan YV]] | ||
| + | [[Category: Rodrigues MJ]] | ||
| + | [[Category: Van Montfort RLM]] | ||
Revision as of 19:46, 11 December 2024
Crystal Structure of HSP72 in complex with ligand 10 at 14.82 MGy X-ray dose.
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