Conformational Mobility Profile of the Active EGFR Dimer.

<p>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 <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0113488#pone-0113488-g003" target="_blank">Figures 3</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0113488#pone-0113488-g004" target="_blank">4</a>. 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.