5mkr

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<StructureSection load='5mkr' size='340' side='right'caption='[[5mkr]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
<StructureSection load='5mkr' size='340' side='right'caption='[[5mkr]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5mkr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MKR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MKR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5mkr]] 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=5MKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MKR FirstGlance]. <br>
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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=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=TI8:3-[(2~{R},3~{S},4~{R},5~{R})-5-[6-AZANYL-8-[(4-CHLOROPHENYL)METHYLAMINO]PURIN-9-YL]-3,4-BIS(OXIDANYL)OXOLAN-2-YL]PROPYL+PROP-2-ENOATE'>TI8</scene></td></tr>
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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]] 1.87&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSPA1A, 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=TI8:3-[(2~{R},3~{S},4~{R},5~{R})-5-[6-AZANYL-8-[(4-CHLOROPHENYL)METHYLAMINO]PURIN-9-YL]-3,4-BIS(OXIDANYL)OXOLAN-2-YL]PROPYL+PROP-2-ENOATE'>TI8</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5mkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkr OCA], [http://pdbe.org/5mkr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mkr RCSB], [http://www.ebi.ac.uk/pdbsum/5mkr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkr ProSAT]</span></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=5mkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkr OCA], [https://pdbe.org/5mkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mkr RCSB], [https://www.ebi.ac.uk/pdbsum/5mkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkr ProSAT]</span></td></tr>
</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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bihan, Y V.Le]]
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[[Category: Cronin N]]
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[[Category: Cronin, N]]
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[[Category: Le Bihan Y-V]]
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[[Category: Montfort, R L.M Van]]
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[[Category: Pettinger J]]
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[[Category: Pettinger, J]]
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[[Category: Van Montfort RLM]]
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[[Category: Westwood, I M]]
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[[Category: Westwood IM]]
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[[Category: Chaperone]]
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[[Category: Irreversible inhibitor]]
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[[Category: Lysine modification]]
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Revision as of 18:48, 1 November 2023

HSP72-NBD bound to compound TCI 8 - Tyr15 in up-conformation

PDB ID 5mkr

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