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Interaction of Hsp70 chaperones with substrates

Nature Structural Biologyvolume 4pages342349 (1997) | Download Citation



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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    • Stefan Rüdiger
    •  & Bernd Bukau

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


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

    • Stefan Rüdiger
    • , Alexander Buchberger
    •  & Bernd Bukau


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