Protein kinases with calmodulin-like domains: novel targets of calcium signals in plants

Curr Opin Cell Biol. 1993 Apr;5(2):242-6. doi: 10.1016/0955-0674(93)90110-c.

Abstract

Recently, a novel calcium-dependent protein kinase has been identified that is structurally distinguished by the localization of a calcium-binding regulatory domain fused to a serine/threonine catalytic domain. The regulatory domain is homologous to calmodulin and contains four helix-loop-helix calcium-binding sites. As a result, the kinase is directly activated by calcium without a requirement for other effector molecules.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Calcium / pharmacology
  • Calmodulin / chemistry*
  • Enzyme Activation / drug effects
  • Molecular Sequence Data
  • Plants / enzymology*
  • Protein Kinases / chemistry*
  • Sequence Homology, Amino Acid

Substances

  • Calmodulin
  • Protein Kinases
  • Calcium