5gjj

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==Glutathionylated hHsp70 SBD==
==Glutathionylated hHsp70 SBD==
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<StructureSection load='5gjj' size='340' side='right' caption='[[5gjj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='5gjj' size='340' side='right'caption='[[5gjj]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5gjj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GJJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GJJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5gjj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GJJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GJJ FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSPA1A, HSP72, HSPA1, HSX70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5gjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gjj OCA], [https://pdbe.org/5gjj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gjj RCSB], [https://www.ebi.ac.uk/pdbsum/5gjj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gjj ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gjj OCA], [http://pdbe.org/5gjj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gjj RCSB], [http://www.ebi.ac.uk/pdbsum/5gjj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gjj ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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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[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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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Gong, W B]]
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[[Category: Large Structures]]
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[[Category: Perrett, S]]
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[[Category: Gong WB]]
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[[Category: Yang, J]]
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[[Category: Perrett S]]
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[[Category: Zhang, H]]
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[[Category: Yang J]]
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[[Category: Chaperone]]
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[[Category: Zhang H]]
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[[Category: Glutathionylation]]
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[[Category: Hsp70]]
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[[Category: Sbd]]
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Revision as of 10:09, 14 June 2023

Glutathionylated hHsp70 SBD

PDB ID 5gjj

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