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. Author manuscript; available in PMC: 2011 Sep 18.
Published in final edited form as: Mol Cell. 2011 Apr 8;42(1):9–22. doi: 10.1016/j.molcel.2011.03.004

Figure 5.

Figure 5

Allosteric control of the EGF receptor dimerization. (A) Schematic representation of the EGF receptor domain organization. (B) The crystal structure and cartoon representation of the EGF receptor kinase (EGFR) domain in the presence of its full juxtamembrane segment (PDB ID: 3GOP) depicts binding of the juxtamembrane latch of the receiver kinase to the activator kinase. (C) The cartoon representation of the overlapping interactions involving the juxtamembrane latch-binding site, based on the structures of the active EGF receptor kinase domain dimer in the presence of its juxtamembrane segment (PDB ID: 3GOP), the inactive EGF receptor kinase dimer (PDB ID: 3GT8) and the inactive EGF receptor kinase bound to an inhibitor Mig6 (PDB ID: 2RFE). (D) The model for ligand-dependent activation of EGF receptor at the plasma membrane, which depicts contribution of the extracellular, transmembrane and the juxtamembrane domains to receptor dimerization.