[HTML][HTML] Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
H Ogiso, R Ishitani, O Nureki, S Fukai, M Yamanaka… - Cell, 2002 - cell.com
H Ogiso, R Ishitani, O Nureki, S Fukai, M Yamanaka, JH Kim, K Saito, A Sakamoto, M Inoue…
Cell, 2002•cell.comEpidermal 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 Å
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 …
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 Å
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 …
Abstract
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 Å 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 β-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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