Conformational Mobility Profile of the Active EGFR Dimer.

Structural distribution of conformational mobility in the asymmetric active dimer of EGFR-WT. In an asymmetric dimer arrangement a donor monomer interacts with an acceptor through interactions involving the αH-helix and αI-helix of the donor as well as the JM-B segment and the αC-helix of the acceptor. The key functional regions are annotated and pointed to by arrows as in Figures 3, 4. Note the increased stability of the acceptor monomer, particularly a uniform stabilization of the R-spine residues in the acceptor subunit. The conformational mobility profiles were mapped onto the original crystal structure of the active EGFR dimer.