1ivo

From Proteopedia

Revision as of 15:28, 12 November 2007

Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains.

Overview

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.

Disease

Known diseases associated with this structure: Adenocarcinoma of lung, response to tyrosine kinase inhibitor in OMIM:[131550], Nonsmall cell lung cancer, response to tyrosine kinase inhibitor in OMIM:[131550], Nonsmall cell lung cancer, susceptibility to OMIM:[131550]

About this Structure

1IVO is a Protein complex structure of sequences from Homo sapiens with NAG as ligand. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.

Reference

Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains., Ogiso H, Ishitani R, Nureki O, Fukai S, Yamanaka M, Kim JH, Saito K, Sakamoto A, Inoue M, Shirouzu M, Yokoyama S, Cell. 2002 Sep 20;110(6):775-87. PMID:12297050

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