Conformational selection in substrate recognition by Hsp70 chaperones.
J Mol Biol
; 425(3): 466-74, 2013 Feb 08.
Article
in En
| MEDLINE
| ID: mdl-23207294
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Molecular Chaperones
/
HSP70 Heat-Shock Proteins
/
Escherichia coli Proteins
/
Escherichia coli
Type of study:
Prognostic_studies
Language:
En
Journal:
J Mol Biol
Year:
2013
Document type:
Article
Affiliation country:
Germany