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Article

Conformational equilibria in allosteric control of Hsp70 chaperones.

Molecular cell - 7 Oct 2021

Wang Wei, Liu Qinglian, Liu Qun, Hendrickson Wayne A

Abstract excerpt

Heat-shock proteins of 70 kDa (Hsp70s) are vital for all life and are notably important in protein folding. Hsp70s use ATP binding and hydrolysis at a nucleotide-binding domain (NBD) to control the binding and release of client polypeptides at a substrate-binding domain (SBD); however, the mechanistic basis for this allostery has been elusive. Here, we first characterize biochemical properties of selected...

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Identifiers

PMID: 34453889
DOI: 10.1016/j.molcel.2021.07.039
PMCID: PMC8500941

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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