View source for 2lgw


==Solution Structure of the J Domain of HSJ1a==
<StructureSection load='2lgw' size='340' side='right'caption='[[2lgw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lgw]] 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=2LGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LGW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgw OCA], [https://pdbe.org/2lgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lgw RCSB], [https://www.ebi.ac.uk/pdbsum/2lgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lgw ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/DNJB2_HUMAN DNJB2_HUMAN] Young adult-onset distal hereditary motor neuropathy. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/DNJB2_HUMAN DNJB2_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lgw" style="background-color:#fffaf0;"></div>

==See Also==
*[[DnaJ homolog 3D structures|DnaJ homolog 3D structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cao C]]
[[Category: Gao X]]
[[Category: Hu H]]
[[Category: Zhou C]]