Peptide-binding specificity of the molecular chaperone BiP

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 u...

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Bibliographic Details
Published in:Nature (London) 1991-10, Vol.353 (6346), p.726-730
Main Authors: Flynn, Gregory C, Pohl, Jan, Flocco, Mark T, Rothman, James E
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
Amino Acid Sequence
Amino Acids - analysis
Binding Sites
Binding, Competitive
Biological and medical sciences
Chemical Phenomena
Chemistry, Physical
Fundamental and applied biological sciences. Psychology
Fungal Proteins - metabolism
Heat-Shock Proteins - metabolism
HSP70 Heat-Shock Proteins
Humanities and Social Sciences
Interactions. Associations
Intermolecular phenomena
Molecular biophysics
Molecular Sequence Data
multidisciplinary
Peptides - chemistry
Peptides - metabolism
Protein Conformation
Science
Science (multidisciplinary)
Thermodynamics
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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/353726a0