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Article

ATP-induced conformational changes in Hsp70: molecular dynamics and experimental validation of an in silico predicted conformation.

Biochemistry - 8 Dec 2009

Woo Hyung-June, Jiang Jianwen, Lafer Eileen M, Sousa Rui

Abstract excerpt

The 70 kDa heat shock proteins (Hsp70s) play important roles in preventing the misfolding of proteins and repairing damage under stress by coupling ATP binding and hydrolysis to protein substrate release and binding, respectively. ATP binding is believed to induce closing of the Hsp70 nucleotide binding domain (NBD) around the nucleotide. We report here a combined computational-experimental study of this...

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Identifiers

PMID: 19883127
DOI: 10.1021/bi901256y
PMCID: PMC2787669

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

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