PMID:9145101
| Citation |
Rüdiger, S, Buchberger, A and Bukau, B (1997) Interaction of Hsp70 chaperones with substrates. Nat. Struct. Biol. 4:342-9 |
|---|---|
| Abstract |
Determination of the structure of the substrate binding domain of the Escherichia coli Hsp70 chaperone, DnaK, and the biochemical characterisation of the motif it recognizes within substrates provide insights into the principles governing Hsp70 interaction with polypeptide chains. DnaK recognizes extended peptide strands composed of up to five consecutive hydrophobic residues within and positively charged residues outside the substrate binding cavity. |
| Links | |
| Keywords |
Binding Sites; Escherichia coli/chemistry; Escherichia coli Proteins; HSP70 Heat-Shock Proteins/chemistry; Models, Molecular; Oligopeptides/chemistry; Protein Conformation; Substrate Specificity |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.