7gy7
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of HSP72 in complex with ligand 10 at 4.56 MGy X-ray dose.== | |
| - | + | <StructureSection load='7gy7' size='340' side='right'caption='[[7gy7]], [[Resolution|resolution]] 1.92Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[7gy7]] 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=7GY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7GY7 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:8-bromoadenosine'>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=7gy7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7gy7 OCA], [https://pdbe.org/7gy7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7gy7 RCSB], [https://www.ebi.ac.uk/pdbsum/7gy7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7gy7 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 19:44, 11 December 2024
Crystal Structure of HSP72 in complex with ligand 10 at 4.56 MGy X-ray dose.
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