Peptide-binding specificity of the molecular chaperone BiP

Nature. 1991 Oct 24;353(6346):726-30. doi: 10.1038/353726a0.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

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
  • Peptides / metabolism*
  • Protein Conformation
  • Thermodynamics

Substances

  • Amino Acids
  • Fungal Proteins
  • HSP70 Heat-Shock Proteins
  • Heat-Shock Proteins
  • KAR2 protein, yeast
  • Peptides
  • Adenosine Triphosphatases