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PMID: 1834945 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Peptide-binding specificity of the molecular chaperone BiP.

Nature ·Vol. 353 ·No. 6346 ·1991-10-24 ·Pages 726-30

Flynn GC, Pohl J, Flocco MT, Rothman JE

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.

MeSH Terms
Adenosine Triphosphatases/metabolism Amino Acid Sequence Amino Acids/analysis Binding Sites Binding, Competitive Chemical Phenomena Chemistry, Physical Fungal Proteins/metabolism HSP70 Heat-Shock Proteins Heat-Shock Proteins/metabolism Molecular Sequence Data Peptides/chemistry,metabolism Protein Conformation Thermodynamics
Chemicals
Amino Acids Fungal Proteins HSP70 Heat-Shock Proteins Heat-Shock Proteins KAR2 protein, yeast Peptides Adenosine Triphosphatases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Flynn G C
Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratory, Sloan-Kettering Institute, New York, New York 10021.
Pohl J
Flocco M T
Rothman J E
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1991-10-24
Pages
726-30
Language
English
Region
England
NLM ID
0410462
Subset
IM
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