EGF receptor activation: push comes to shove

Cell. 2006 Jun 16;125(6):1029-31. doi: 10.1016/j.cell.2006.05.028.

Abstract

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.

Publication types

  • Comment

MeSH terms

  • Allosteric Regulation
  • Animals
  • Cyclin-Dependent Kinases / chemistry
  • Dimerization
  • Enzyme Activation
  • ErbB Receptors / chemistry
  • ErbB Receptors / genetics
  • ErbB Receptors / metabolism*
  • Humans
  • Mice
  • Models, Molecular*
  • Mutation
  • Phosphorylation
  • Protein Conformation
  • Protein Structure, Tertiary
  • src-Family Kinases / chemistry

Substances

  • ErbB Receptors
  • src-Family Kinases
  • Cyclin-Dependent Kinases