Title : 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
Output (sent_index, trigger,
protein,
sugar,
site):
Output(Part-Of) (sent_index,
protein,
site):
- 1. EGF receptor, region
- 2. EGF, region
- 2. EGFR, region
- 3. EGFR, domains
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):