PMID:23207294

Citation	Marcinowski, M, Rosam, M, Seitz, C, Elferich, J, Behnke, J, Bello, C, Feige, MJ, Becker, CF, Antes, I and Buchner, J (2013) Conformational selection in substrate recognition by Hsp70 chaperones. J. Mol. Biol. 425:466-74
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.
Links	PubMed Online version:10.1016/j.jmb.2012.11.030
Keywords	Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; HSP70 Heat-Shock Proteins/chemistry; HSP70 Heat-Shock Proteins/metabolism; Kinetics; Models, Molecular; Molecular Chaperones/chemistry; Molecular Chaperones/metabolism; Protein Binding; Substrate Specificity
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.