Targeting the Epidermal Growth Factor Receptor in Epithelial Ovarian Cancer: Current Knowledge and Future Challenges

Figure 1

Structure of EGFR. EGFR consists of extracellular, transmembrane, and intracellular domains. The extracellular domain is the least conserved domain among the EGFR family members and consists of 4 subdomains—two ligand-binding domains and two receptor dimerization domains, which are cysteine-rich (reviewed in [12]). The transmembrane domain, which spans the cell membrane, is hydrophobic. The cytoplasmic tail of the EGFR family is highly conserved and contains the tyrosine kinase domain. Activation of EGFR family members leads to autophosphorylation of the tyrosine residues in the cytoplasmic tail. The phosphorylated tyrosine residues become docking sites for proteins with SRC homology 2 and phosphotyrosine binding domains, which transduce the signals downstream. EGFR phosphorylation at selected residues and their functional outcomes are indicted in the diagram. T: threonine; Y: tyrosine.