Different peptide binding specificities of hsp70 family members

J Mol Biol. 1994 Aug 12;241(2):133-5. doi: 10.1006/jmbi.1994.1482.

Abstract

A set of heptapeptides was used to compare the relative peptide affinities of three proteins of the hsp70 family: bacterial DnaK, mammalian cytosolic hsc70, and BiP from mammalian ER. Each hsp displays a characteristic pattern of relative affinities. DnaK and hsc70 are more similar to each other than to BiP. A difference in peptide binding specificity may be an important determinant in adjusting an hsp70 family member to its particular cellular function.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism*
  • Cattle
  • Cricetinae
  • Escherichia coli Proteins*
  • Fungal Proteins / metabolism*
  • HSP70 Heat-Shock Proteins*
  • Heat-Shock Proteins / metabolism*
  • Molecular Sequence Data
  • Oligopeptides / metabolism
  • Protein Binding
  • Recombinant Proteins / metabolism

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Fungal Proteins
  • HSP70 Heat-Shock Proteins
  • Heat-Shock Proteins
  • KAR2 protein, yeast
  • Oligopeptides
  • Recombinant Proteins
  • dnaK protein, E coli