EGF receptor activation: push comes to shove.
A study by Zhang et al. (2006) in this issue of Cell provides compelling evidence that the tyrosine kinase domain of the epidermal growth factor receptor (EGFR) is activated by the formation of an asymmetric dimer, with one kinase domain in the EGF-mediated dimer activating the other through an allosteric mechanism.
Hubbard
Stevan R
SR
Structural Biology Program, Skirball Institute of Biomolecular Medicine, and Department of Pharmacology, New York University School of Medicine, New York, NY 10016, USA.
D000494:Allosteric Regulation; D000818:Animals; D018844:Cyclin-Dependent Kinases / Q000737:chemistry; D019281:Dimerization; D004789:Enzyme Activation; D066246:ErbB Receptors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D009154:Mutation; D010766:Phosphorylation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D019061:src-Family Kinases / Q000737:chemistry
D066246:ErbB Receptors; D019061:src-Family Kinases; D018844:Cyclin-Dependent Kinases