7gyc

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m (Protected "7gyc" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 7gyc is ON HOLD
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==Crystal Structure of HSP72 in complex with ligand 10 at 10.26 MGy X-ray dose.==
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<StructureSection load='7gyc' size='340' side='right'caption='[[7gyc]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7gyc]] 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=7GYC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7GYC FirstGlance]. <br>
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Description:
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7gyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7gyc OCA], [https://pdbe.org/7gyc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7gyc RCSB], [https://www.ebi.ac.uk/pdbsum/7gyc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7gyc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Cabry M]]
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[[Category: Le Bihan YV]]
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[[Category: Rodrigues MJ]]
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[[Category: Van Montfort RLM]]

Revision as of 19:45, 11 December 2024

Crystal Structure of HSP72 in complex with ligand 10 at 10.26 MGy X-ray dose.

PDB ID 7gyc

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