A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase

M. Osawa, H. Tokumitsu, M. B. Swindells, H. Kurihara, M. Orita, T. Shibanuma, T. Furuya, M. Ikura

Research output: Contribution to journalArticlepeer-review

224 Citations (Scopus)


The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a 26-residue peptide, corresponding to the CaM-binding domain of rat Ca2+/CaM-dependent protein kinase kinase (CaMKK), has been determined by NMR spectroscopy. In this complex, the CaMKK peptide forms a fold comprising an α-helix and a hairpin-like loop whose C-terminus folds back on itself. The binding orientation of this CaMKK peptide by the two CaM domains is opposite to that observed in all other CaM-target complexes determined so far. The N- and C-terminal hydrophobic pockets of Ca2+/CaM anchor Trp 444 and Phe 459 of the CaMKK peptide, respectively. This 14-residue separation between two key hydrophobic groups is also unique among previously determined CaM complexes. The present structure represents a new and distinct class of Ca2+/CaM target recognition that may be shared by other Ca2+/CaM- stimulated proteins.

Original languageEnglish
Pages (from-to)819-824
Number of pages6
JournalNature Structural Biology
Issue number9
Publication statusPublished - 1999
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics


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