Protein-protein interactions in the allosteric regulation of protein kinases

Curr Opin Struct Biol. 2006 Dec;16(6):702-9. doi: 10.1016/j.sbi.2006.10.007. Epub 2006 Oct 31.

Abstract

Protein-protein interactions involving the catalytic domain of protein kinases are likely to be generally important in the regulation of signal transduction pathways, but are rather sparsely represented in crystal structures. Recently determined structures of the kinase domains of the mitogen-activated protein kinase Fus3, the RNA-dependent kinase PKR, the epidermal growth factor receptor and Ca(2+)/calmodulin-dependent protein kinase II have revealed unexpected and distinct mechanisms by which interactions with the catalytic domain can modulate kinase activity.

Publication types

  • Review

MeSH terms

  • Allosteric Regulation
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinases / chemistry
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism
  • Dimerization
  • ErbB Receptors / chemistry
  • ErbB Receptors / metabolism
  • Models, Molecular
  • Multiprotein Complexes
  • Protein Binding
  • Protein Kinases / chemistry*
  • Protein Kinases / metabolism*
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary

Substances

  • Multiprotein Complexes
  • Protein Kinases
  • ErbB Receptors
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinases