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5ar0

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==HSP72 with adenosine-derived inhibitor==
==HSP72 with adenosine-derived inhibitor==
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<StructureSection load='5ar0' size='340' side='right' caption='[[5ar0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='5ar0' size='340' side='right'caption='[[5ar0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ar0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AR0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AR0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ar0]] 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=5AR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AR0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GB8:(2R,3R,4S,5R)-2-(6-AMINO-8-((QUINOLIN-7-YLMETHYL)AMINO)-9H-PURIN-9-YL)-5-(HYDROXYMETHYL)TETRAHYDROFURAN-3,4-DIOL'>GB8</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5aqf|5aqf]], [[5aqg|5aqg]], [[5aqh|5aqh]], [[5aqi|5aqi]], [[5aqj|5aqj]], [[5aqk|5aqk]], [[5aql|5aql]], [[5aqm|5aqm]], [[5aqn|5aqn]], [[5aqo|5aqo]], [[5aqp|5aqp]], [[5aqq|5aqq]], [[5aqr|5aqr]], [[5aqs|5aqs]], [[5aqt|5aqt]], [[5aqu|5aqu]], [[5aqv|5aqv]], [[5aqw|5aqw]], [[5aqx|5aqx]], [[5aqy|5aqy]], [[5aqz|5aqz]]</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GB8:(2R,3R,4S,5R)-2-(6-AMINO-8-((QUINOLIN-7-YLMETHYL)AMINO)-9H-PURIN-9-YL)-5-(HYDROXYMETHYL)TETRAHYDROFURAN-3,4-DIOL'>GB8</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mitochondrial_protein-transporting_ATPase Mitochondrial protein-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.51 3.6.3.51] </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=5ar0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ar0 OCA], [https://pdbe.org/5ar0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ar0 RCSB], [https://www.ebi.ac.uk/pdbsum/5ar0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ar0 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=5ar0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ar0 OCA], [http://pdbe.org/5ar0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ar0 RCSB], [http://www.ebi.ac.uk/pdbsum/5ar0 PDBsum]</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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5ar0" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5ar0" style="background-color:#fffaf0;"></div>
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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: Mitochondrial protein-transporting ATPase]]
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[[Category: Homo sapiens]]
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[[Category: Barbeau, O]]
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[[Category: Large Structures]]
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[[Category: Burke, R]]
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[[Category: Barbeau O]]
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[[Category: Cheeseman, M D]]
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[[Category: Burke R]]
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[[Category: Collins, I]]
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[[Category: Cheeseman MD]]
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[[Category: Dobson, S E]]
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[[Category: Collins I]]
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[[Category: Jeganathan, F]]
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[[Category: Dobson SE]]
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[[Category: Jones, A M]]
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[[Category: Jeganathan F]]
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[[Category: Jones, K]]
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[[Category: Jones AM]]
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[[Category: Montfort, R L.M van]]
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[[Category: Jones K]]
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[[Category: Rowlands, M G]]
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[[Category: Rowlands MG]]
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[[Category: Westwood, I M]]
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[[Category: Westwood IM]]
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[[Category: Workman, P]]
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[[Category: Workman P]]
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[[Category: Adenosine]]
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[[Category: Van Montfort RLM]]
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[[Category: Atpase]]
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[[Category: Chaperone]]
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[[Category: Heat shock protein]]
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[[Category: Hsp70]]
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[[Category: Hsp72]]
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[[Category: Inhibitor]]
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Current revision

HSP72 with adenosine-derived inhibitor

PDB ID 5ar0

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