作者: I Lax , W H Burgess , F Bellot , A Ullrich , J Schlessinger
DOI: 10.1128/MCB.8.4.1831
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摘要: Epidermal growth factor (EGF) receptor was affinity labeled with 125I-labeled EGF, using bifunctional covalent cross-linking agents. The affinity-labeled isolated and cleaved CNBr to yield a single-labeled fragment, which unequivocally identified by site-specific antibodies other methods encompass residues 294 543 of the EGF receptor. On basis amino acid sequence conservation, extracellular portion can be divided into four domains. fragment contains entire is flanked two cysteine-rich domains denoted as domain III. these results, we propose that III contributes most interactions define ligand-binding specificity