title: Interaction of Hsp70 chaperones with substrates.
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.
authors.affiliation: Zentrum für Molekulare Biologie, Universität Heidelberg, Germany.
authors.forename: S
authors.initials: S
authors.lastname: Rüdiger
authors.forename: A
authors.initials: A
authors.lastname: Buchberger
authors.forename: B
authors.initials: B
authors.lastname: Bukau
mesh_terms: D001665:Binding Sites; D004926:Escherichia coli / Q000737:chemistry; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry*; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry; D011487:Protein Conformation; D013379:Substrate Specificity
chemical_list: D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D009842:Oligopeptides; C063842:dnaK protein, E coli