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An unexpected second binding site for polypeptide substrates is essential for Hsp70 chaperone activity

Heat shock proteins of 70 kDa (Hsp70s) are ubiquitous and highly conserved molecular chaperones. They play multiple essential roles in assisting with protein folding and maintaining protein homeostasis. Their chaperone activity has been proposed to require several rounds of binding to and release of...

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Vydáno v:J Biol Chem
Hlavní autoři: Li, Hongtao, Zhu, Huanyu, Sarbeng, Evans Boateng, Liu, Qingdai, Tian, Xueli, Yang, Ying, Lyons, Charles, Zhou, Lei, Liu, Qinglian
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2020
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC6956537/
https://ncbi.nlm.nih.gov/pubmed/31806707
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA119.009686
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