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Article

Mechanics of Hsp70 chaperones enables differential interaction with client proteins.

Nature structural & molecular biology - 1 Mar 2011

Schlecht Rainer, Erbse Annette H, Bukau Bernd, Mayer Matthias P

Abstract excerpt

Hsp70 chaperones interact with a wide spectrum of substrates ranging from unfolded to natively folded and aggregated proteins. Structural evidence suggests that bound substrates are entirely enclosed in a β-sheet cavity covered by a helical lid, which requires structural rearrangements including lid opening to allow substrate access. We analyzed the mechanics of the lid movement of bacterial DnaK by disulfide...

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Identifiers

PMID: 21278757
DOI: 10.1038/nsmb.2006

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Mechanics of Hsp70 chaperones enables differential interaction with client proteins.PMID 21278757Read ↗

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