Open AccessLocalization of a major receptor-binding domain for epidermal growth factor by affinity labeling.
Author(s) -
Irit Lax,
W H Burgess,
F Bellot,
A Ullrich,
Joseph Schlessinger,
David Givol
Publication year - 1988
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.8.4.1831
Subject(s) - biology , epidermal growth factor , receptor , extracellular , peptide sequence , biochemistry , insulin like growth factor 2 receptor , epidermal growth factor receptor , egf like domain , cysteine , microbiology and biotechnology , 5 ht5a receptor , binding site , binding domain , growth factor , insulin like growth factor 1 receptor , enzyme , gene
Epidermal growth factor (EGF) receptor was affinity labeled with 125I-labeled EGF, using bifunctional covalent cross-linking agents. The affinity-labeled receptor was isolated and cleaved with CNBr to yield a single-labeled fragment, which was unequivocally identified by site-specific antibodies and other methods to encompass residues 294 to 543 of the EGF receptor. On the basis of amino acid sequence conservation, the extracellular portion of EGF receptor can be divided into four domains. The labeled CNBr fragment contains the entire sequence which is flanked by the two cysteine-rich domains of extracellular portion of the EGF receptor denoted as domain III. On the basis of these and other results, we propose that domain III contributes most of the interactions that define ligand-binding specificity of the EGF receptor.