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. 2002 Sep 20;110(6):775-87.
doi: 10.1016/s0092-8674(02)00963-7.

Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains

Hideo Ogiso  1 , Ryuichiro Ishitani, Osamu Nureki, Shuya Fukai, Mari Yamanaka, Jae-Hoon Kim, Kazuki Saito, Ayako Sakamoto, Mio Inoue, Mikako Shirouzu, Shigeyuki Yokoyama
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Free article

Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains

Hideo Ogiso et al. Cell. .
Free article

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 A 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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