Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase. In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 Angstrom resolution. EGFR domains I-III are arranged in a C shape, and EGF is docked between domains I and III. The 1:1 EGF.EGFR complex dimerizes through a direct receptor.receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other. The unique receptor-mediated dimerization was verified by EGFR mutagenesis.
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