4wv5: Difference between revisions
New page: '''Unreleased structure''' The entry 4wv5 is ON HOLD until Paper Publication Authors: Kirby, C., Stams, T., Baird, J. Description: HEAT SHOCK PROTEIN 70 SUBSTRATE BINDING DOMAIN |
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==HEAT SHOCK PROTEIN 70 SUBSTRATE BINDING DOMAIN== | |||
<StructureSection load='4wv5' size='340' side='right'caption='[[4wv5]], [[Resolution|resolution]] 2.04Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4wv5]] is a 2 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=4WV5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WV5 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]] 2.04Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4wv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wv5 OCA], [https://pdbe.org/4wv5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wv5 RCSB], [https://www.ebi.ac.uk/pdbsum/4wv5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wv5 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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The highly conserved 70 kDa heat shock proteins (Hsp70) play an integral role in proteostasis such that dysregulation has been implicated in numerous diseases. Elucidating the precise role of Hsp70 family members in the cellular context, however, has been hampered by the redundancy and intricate regulation of the chaperone network, and relatively few selective and potent tools. We have characterized a natural product, novolactone, that targets cytosolic and ER-localized isoforms of Hsp70 through a highly conserved covalent interaction at the interface between the substrate-binding and ATPase domains. Biochemical and structural analyses indicate that novolactone disrupts interdomain communication by allosterically inducing a conformational change in the Hsp70 protein to block ATP-induced substrate release and inhibit refolding activities. Thus, novolactone is a valuable tool for exploring the requirements of Hsp70 chaperones in diverse cellular contexts. | |||
The Novolactone Natural Product Disrupts the Allosteric Regulation of Hsp70.,Hassan AQ, Kirby CA, Zhou W, Schuhmann T, Kityk R, Kipp DR, Baird J, Chen J, Chen Y, Chung F, Hoepfner D, Movva NR, Pagliarini R, Petersen F, Quinn C, Quinn D, Riedl R, Schmitt EK, Schitter A, Stams T, Studer C, Fortin PD, Mayer MP, Sadlish H Chem Biol. 2014 Dec 23. pii: S1074-5521(14)00415-3. doi:, 10.1016/j.chembiol.2014.11.007. PMID:25544045<ref>PMID:25544045</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4wv5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Baird J]] | |||
[[Category: Kirby C]] | |||
[[Category: Stams T]] | |||