Open AccessMapping of Hsp70‐binding sites on protein antigens
Author(s) -
ROMÁN Eulogia,
MORENO Carlos,
YOUNG Douglas
Publication year - 1994
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1994.tb18842.x
Subject(s) - peptide , amino acid , binding site , biochemistry , antigen , biology , hsp70 , peptide sequence , binding protein , chemistry , microbiology and biotechnology , heat shock protein , immunology , gene
Hsp70‐binding sites were mapped on three antigens, the 16‐, 19‐ and 38‐kDa proteins of Myco‐bacterium tuberculosis , using overlapping synthetic peptides in a competitive‐binding assay. In each protein, two or three prominent hsp70‐binding sites were identified when peptides 20‐amino‐acid long were used, predominantly in regions containing clusters of aliphatic amino acids. Although there was an overall concordance in the pattern of peptide binding to hsp70 from bacterial ( M. tuberculosis ) and mammalian sources (immunoglobulin heavy‐chain‐binding protein), some differences in the specificity of polypeptide binding and the effect of peptides on ATPase activity were observed.