Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane Segment

Abstract

(Cell 137, 1293–1307; June 26, 2009) In the print and original online versions of this article, the Protein Data Bank code was incorrectly cited as 3GTS. The correct PDB code is 3GT8. The error has been corrected in the version that now appears online. Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane SegmentJura et al.CellJune 26, 2009In BriefSignaling by the epidermal growth factor receptor requires an allosteric interaction between the kinase domains of two receptors, whereby one activates the other. We show that the intracellular juxtamembrane segment of the receptor, known to potentiate kinase activity, is able to dimerize the kinase domains. The C-terminal half of the juxtamembrane segment latches the activated kinase domain to the activator, and the N-terminal half of this segment further potentiates dimerization, most likely by forming an antiparallel helical dimer that engages the transmembrane helices of the activated receptor. Full-Text PDF Open Archive