2lgw
From Proteopedia
Solution Structure of the J Domain of HSJ1a
Structural highlights
DiseaseDNJB2_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. FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Homo sapiens | Large Structures | Cao C | Gao X | Hu H | Zhou C