1IVO: Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains

Citation:
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.
PDB ID: 1IVODownload
MMDB ID: 20809
PDB Deposition Date: 2002/3/28
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 3.3  Å
Source Organism:
Similar Structures:
Biological Unit for 1IVO: tetrameric; determined by author and by software (PISA)
Molecular Components in 1IVO
Label Count Molecule
Proteins (4 molecules)
2
Epidermal Growth Factor Receptor(Gene symbol: EGFR)
Molecule annotation
2
Epidermal Growth Factor(Gene symbol: EGF)
Molecule annotation
Chemicals (10 molecules)
1
10
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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