The conformational plasticity of protein kinases

Cell. 2002 May 3;109(3):275-82. doi: 10.1016/s0092-8674(02)00741-9.

Abstract

Protein kinases operate in a large number of distinct signaling pathways, where the tight regulation of their catalytic activity is crucial to the development and maintenance of eukaryotic organisms. The catalytic domains of different kinases adopt strikingly similar structures when they are active. By contrast, crystal structures of inactive kinases have revealed a remarkable plasticity in the kinase domain that allows the adoption of distinct conformations in response to interactions with specific regulatory domains or proteins.

Publication types

  • Review

MeSH terms

  • Animals
  • Catalytic Domain / physiology
  • Enzyme Activation
  • Eukaryotic Cells / enzymology
  • Models, Molecular
  • Protein Conformation
  • Protein Kinases / chemistry
  • Protein Kinases / metabolism*
  • Protein-Serine-Threonine Kinases / metabolism
  • Receptor Protein-Tyrosine Kinases / metabolism
  • Receptor, EphB2
  • Receptor, Transforming Growth Factor-beta Type I
  • Receptors, Transforming Growth Factor beta
  • Signal Transduction
  • Substrate Specificity

Substances

  • Receptors, Transforming Growth Factor beta
  • Protein Kinases
  • Receptor Protein-Tyrosine Kinases
  • Receptor, EphB2
  • Protein-Serine-Threonine Kinases
  • Receptor, Transforming Growth Factor-beta Type I