Conformational Mobility Profile of the Active EGFR Dimer.
figureposted on 2014-11-26, 02:44 authored by Kevin A. James, Gennady M. Verkhivker
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.
dynamicstabilityreceptor tyrosine kinasesoncogenic EGFR dimershrdallostericsubstrate binding siteRegulatory Spine Residuescommunicationatpresidue interaction networksdfgsubstrate binding regionErbB kinasesprotein structure networknucleotide binding siteprotein structure network modelingnmrErbB protein tyrosine kinases