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Interaction of Hsp70 chaperones with substrates

Nature Structural Biology volume 4, pages 342–349 (1997)Cite this article

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.

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  1. Stefan Rüdiger & Bernd Bukau

    Present address: Institut für Biochemieand Molekularbiologie, Universität Freiburg, Hermann Herder Str. 7, D-79104, Freiburg, Germany

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  1. Zentrum füur MolekulareBiologie, Universität Heidelberg, INF 282, D69120, Heidelberg, Germany

    Stefan Rüdiger, Alexander Buchberger & Bernd Bukau

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Rüdiger, S., Buchberger, A. & Bukau, B. Interaction of Hsp70 chaperones with substrates. Nat Struct Mol Biol 4, 342–349 (1997). https://doi.org/10.1038/nsb0597-342

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