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

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

Cell

journal_title

Cell

authors

Ogiso H,Ishitani R,Nureki O,Fukai S,Yamanaka M,Kim JH,Saito K,Sakamoto A,Inoue M,Shirouzu M,Yokoyama S

doi

10.1016/s0092-8674(02)00963-7

subject

Has Abstract

pub_date

2002-09-20 00:00:00

pages

775-87

issue

6

eissn

0092-8674

issn

1097-4172

pii

S0092867402009637

journal_volume

110

pub_type

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