Conformational requirements for Ca2+/calmodulin binding and activation of myosin light chain kinase

Roanna C. Padre, James T. Stull

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

Myosin light chain kinase contains a regulatory segment consisting of an autoinhibitory region and a calmodulin-binding sequence that folds back on its catalytic core to inhibit kinase activity. It has been proposed that α-helix formation may be involved in displacement of the regulatory segment and activation of the kinase by Ca2+/calmodulin. Proline mutations were introduced at putative non-interacting residues in the regulatory segment to disrupt helix formation. Substitution of proline residues immediately N-terminal of the Trp in the calmodulin-binding sequence had most significant effects on Ca2+/calmodulin binding and activation. Formation of an α-helix in this region upon Ca2+/calmodulin binding may be necessary for displacement of the regulatory segment allowing phosphorylation of myosin regulatory light chain. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)148-152
Number of pages5
JournalFEBS Letters
Volume472
Issue number1
DOIs
StatePublished - Apr 21 2000

Keywords

  • Activation
  • Autoinhibition
  • Calmodulin
  • Helix
  • Myosin light chain kinase
  • Proline

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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