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. Author manuscript; available in PMC: 2018 Sep 1.
Published in final edited form as: Biochim Biophys Acta. 2016 Dec 24;1859(9 Pt A):1430–1435. doi: 10.1016/j.bbamem.2016.12.015

Figure 4.

Figure 4

Steps in EGFR activation. (a) Inactive EGFR. (b) EGFR is activated upon ligand binding. This induces a conformational change in extracellular domains I, II, and III. (c) The activated receptor dimerizes with another EGFR monomer driven by extracellular interactions. Domains I and II contribute to the binding site for EGF, and domain II contributes the dimerization interface; binding of a single EGF ligand to the activated dimer represents negative cooperativity when EGFR is in this state [2]. (d) Intracellular region then assumes the asymmetric kinase conformation. (e) The receiving receptor (blue) trans-phosphorylates tyrosine residues in the activating receptor’s (red) tail region.