Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR

Tapas K. Mal, Nikolai R. Skrynnikov, Kyoko L. Yap, Lewis E. Kay, Mitsuhiko Ikura

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Calmodulin-regulated serine/threonine kinases (CaM kinases) play crucial roles in Ca2+-dependent signaling transduction pathways in eukaryotes. Despite having a similar overall molecular architecture of catalytic and regulatory domains, CaM kinases employ different binding modes for Ca2+/CaM recruitment which is required for their activation. Here we present a residual dipolar coupling (RDC)-based NMR approach to characterizing the molecular recognition of CaM with five different CaM kinases. Our analyses indicate that CaM kinase I and likely IV use the same CaM binding mode as myosin light chain kinase (1-14 motif), distinct from those of CaM kinase II (1-10 motif) and CaM kinase kinase (1-16- motif). This NMR approach provides an efficient experimental guide for homology modeling and structural characterization of CaM - target complexes.

Original languageEnglish (US)
Pages (from-to)12899-12906
Number of pages8
JournalBiochemistry
Volume41
Issue number43
DOIs
StatePublished - Oct 29 2002

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Protein-Serine-Threonine Kinases
Calmodulin
Protein Kinases
Nuclear magnetic resonance
Myosin-Light-Chain Kinase
Molecular recognition
Eukaryota
Catalytic Domain
Phosphotransferases
Chemical activation

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Mal, Tapas K. ; Skrynnikov, Nikolai R. ; Yap, Kyoko L. ; Kay, Lewis E. ; Ikura, Mitsuhiko. / Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR. In: Biochemistry. 2002 ; Vol. 41, No. 43. pp. 12899-12906.
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Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR. / Mal, Tapas K.; Skrynnikov, Nikolai R.; Yap, Kyoko L.; Kay, Lewis E.; Ikura, Mitsuhiko.

In: Biochemistry, Vol. 41, No. 43, 29.10.2002, p. 12899-12906.

Research output: Contribution to journalArticle

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