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J Mol Biol. 2013 Feb 8;425(3):466-74. doi: 10.1016/j.jmb.2012.11.030. Epub 2012 Dec 1.

Conformational selection in substrate recognition by Hsp70 chaperones.

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  • 1Department Chemie, Technische Universität München, 85748 Garching, Germany.

Abstract

Hsp70s are molecular chaperones involved in the folding and assembly of proteins. They recognize hydrophobic amino acid stretches in their substrate binding groove. However, a detailed understanding of substrate specificity is still missing. Here, we use the endoplasmic reticulum-resident Hsp70 BiP to identify binding sites in a natural client protein. Two sites are mutually recognized and form stable Hsp70-substrate complexes. In silico and in vitro analyses revealed an extended substrate conformation as a crucial factor for interaction and show an unexpected plasticity of the substrate binding groove. The basic binding mechanism is conserved among different Hsp70s.

Copyright © 2012 Elsevier Ltd. All rights reserved.

PMID:
23207294
[PubMed - indexed for MEDLINE]
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