2lmg

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[[Image:2lmg.png|left|200px]]
 
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==Solution Structure of The C-terminal Domain (537-610) of Human Heat Shock Protein 70==
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The line below this paragraph, containing "STRUCTURE_2lmg", creates the "Structure Box" on the page.
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<StructureSection load='2lmg' size='340' side='right'caption='[[2lmg]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2lmg]] 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=2LMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LMG FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=2lmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lmg OCA], [https://pdbe.org/2lmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lmg RCSB], [https://www.ebi.ac.uk/pdbsum/2lmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lmg ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_2lmg| PDB=2lmg | SCENE= }}
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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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The J-domain co-chaperones work together with the heat shock protein 70 (HSP70) chaperone to regulate many cellular events, but the mechanism underlying the J-domain-mediated HSP70 function remains elusive. We studied the interaction between human-inducible HSP70 and Homo sapiens J-domain protein (HSJ1a), a J domain and UIM motif-containing co-chaperone. The J domain of HSJ1a shares a conserved structure with other J domains from both eukaryotic and prokaryotic species, and it mediates the interaction with and the ATPase cycle of HSP70. Our in vitro study corroborates that the N terminus of HSP70 including the ATPase domain and the substrate-binding beta-subdomain is not sufficient to bind with the J domain of HSJ1a. The C-terminal helical alpha-subdomain of HSP70, which was considered to function as a lid of the substrate-binding domain, is crucial for binding with the J domain of HSJ1a and stimulating the ATPase activity of HSP70. These fluctuating helices are likely to contribute to a proper conformation of HSP70 for J-domain binding other than directly bind with the J domain. Our findings provide an alternative mechanism of allosteric activation for functional regulation of HSP70 by its J-domain co-chaperones.
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===Solution Structure of The C-terminal Domain (537-610) of Human Heat Shock Protein 70===
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The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation.,Gao XC, Zhou CJ, Zhou ZR, Wu M, Cao CY, Hu HY J Biol Chem. 2012 Feb 17;287(8):6044-52. Epub 2012 Jan 3. PMID:22219199<ref>PMID:22219199</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2lmg" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[2lmg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LMG OCA].
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Gao, X.]]
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[[Category: Large Structures]]
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[[Category: Hu, H.]]
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[[Category: Gao X]]
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[[Category: Wu, M.]]
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[[Category: Hu H]]
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[[Category: Zhou, C.]]
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[[Category: Wu M]]
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[[Category: Chaperone]]
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[[Category: Zhou C]]
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[[Category: Helix]]
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[[Category: Hsp70]]
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Current revision

Solution Structure of The C-terminal Domain (537-610) of Human Heat Shock Protein 70

PDB ID 2lmg

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