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.
journal_name
Celljournal_title
Cellauthors
Ogiso H,Ishitani R,Nureki O,Fukai S,Yamanaka M,Kim JH,Saito K,Sakamoto A,Inoue M,Shirouzu M,Yokoyama Sdoi
10.1016/s0092-8674(02)00963-7subject
Has Abstractpub_date
2002-09-20 00:00:00pages
775-87issue
6eissn
0092-8674issn
1097-4172pii
S0092867402009637journal_volume
110pub_type
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