Ontology highlight
ABSTRACT:
SUBMITTER: Li H
PROVIDER: S-EPMC6956537 | biostudies-literature | 2020 Jan
REPOSITORIES: biostudies-literature
Li Hongtao H Zhu Huanyu H Sarbeng Evans Boateng EB Liu Qingdai Q Tian Xueli X Yang Ying Y Lyons Charles C Zhou Lei L Liu Qinglian Q
The Journal of biological chemistry 20191205 2
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 polypeptide substrates at the substrate-binding domain (SBD) of Hsp70s. All available structures have revealed a single substrate-binding site in the SBD that binds a single segment of an extended po ...[more]