Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms

Mol Cell. 2011 Apr 8;42(1):9-22. doi: 10.1016/j.molcel.2011.03.004.


In contrast to the active conformations of protein kinases, which are essentially the same for all kinases, inactive kinase conformations are structurally diverse. Some inactive conformations are, however, observed repeatedly in different kinases, perhaps reflecting an important role in catalysis. In this review, we analyze one of these recurring conformations, first identified in CDK and Src kinases, which turned out to be central to understanding of how kinase domain of the EGF receptor is activated. This mechanism, which involves the stabilization of the active conformation of an α helix, has features in common with mechanisms operative in several other kinases.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Allosteric Regulation
  • Catalysis
  • Cyclin-Dependent Kinases / chemistry
  • Cyclin-Dependent Kinases / metabolism
  • Dimerization
  • Enzyme Activation
  • Enzyme Stability
  • ErbB Receptors / chemistry*
  • ErbB Receptors / metabolism*
  • Humans
  • Models, Biological
  • Models, Molecular
  • Protein Conformation
  • Protein Kinases / chemistry
  • Protein Kinases / metabolism
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • src-Family Kinases / chemistry
  • src-Family Kinases / metabolism


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