Journal article
Characterization of a comparative model of the extracellular domain of the epidermal growth factor receptor
RN Jorissen, VC Epa, HR Treutlein, TPJ Garrett, CW Ward, AW Burgess
Protein Science | CAMBRIDGE UNIV PRESS | Published : 2000
DOI: 10.1110/ps.9.2.310
Abstract
The Epidermal Growth Factor (EGF) receptor is a tyrosine kinase that mediates the biological effects of ligands such as EGF and transforming growth factor alpha. An understanding of the molecular basis of its action has been hindered by a lack of structural and mutational data on the receptor. We have constructed comparative models of the four extracellular domains of the EGF receptor that are based on the structure of the first three domains of the insulin-like growth factor-1 (IGF-1) receptor. The first and third domains of the EGF receptor, L1 and L2, are right-handed beta helices. The second and fourth domains of the EGF receptor, S1 and S2, consist of the modules held together by disulf..
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