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Peptide-binding specificity of the molecular chaperone BiP

Nature volume 353, pages 726–730 (1991)Cite this article

Abstract

Members of the heat-shock protein family (hsp70s) can distinguish folded from unfolded proteins. This property is crucial to the role of hsp70s as molecular chaperones and is attributable to the amino-acid specificity of the peptide-binding site. The specificity for peptide ligands is investigated using a set of peptides of random sequence but defined chain length. The peptide-binding site selects for aliphatic residues and accommodates them in an environment energetically equivalent to the interior of a folded protein.

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Author notes

  1. Jan Pohl: Microchemical Facility, Emory University School of Medicine, Atlanta, Georgia 30322, USA

  2. Mark T. Flocco: Microchemistry Core Facility, Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA

Authors and Affiliations

  1. Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratory, Sloan-Kettering Institute, 1275 York Avenue, New York, New York, 10021, USA

    Gregory C. Flynn, Jan Pohl, Mark T. Flocco & James E. Rothman

Authors
  1. Gregory C. Flynn
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  2. Jan Pohl
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  3. Mark T. Flocco
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  4. James E. Rothman
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Flynn, G., Pohl, J., Flocco, M. et al. Peptide-binding specificity of the molecular chaperone BiP. Nature 353, 726–730 (1991). https://doi.org/10.1038/353726a0

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