Drug binding by calmodulin: crystal structure of a...[Biochemistry. 1994]

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1: Biochemistry. 1994 Dec 27;33(51):15259-65.Links

Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex.

Cook WJ, Walter LJ, Walter MR.

Department of Pathology, University of Alabama at Birmingham 35294.

The crystal structure of calmodulin (CaM) bound to trifluoperazine (TFP) has been determined and refined to a resolution of 2.45 A. Only one TFP is bound to CaM, but that is sufficient to cause distortion of the central alpha-helix and juxtaposition of the N- and C-terminal domains similar to that seen in CaM-polypeptide complexes. The drug makes extensive contacts with residues in the C-terminal domain of CaM but only a few contacts with one residue in the N-terminal domain. The structure suggests that substrate binding to the C-terminal domain is sufficient to cause the conformational changes in calmodulin that lead to activation of its targets.

PMID: 7803388 [PubMed - indexed for MEDLINE]

Molecular dynamics simulation of the calmodulin-trifluoperazine complex in aqueous solution. [Biopolymers. 2001]
The structure of the complex of calmodulin with KAR-2: a novel mode of binding explains the unique pharmacology of the drug. [J Biol Chem. 2005]
Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: studies of the kinase activation mechanism. [Biochemistry. 2002]
ReviewStructure, dynamics and interaction with kinase targets: computer simulations of calmodulin. [Biochim Biophys Acta. 2004]
ReviewMolecular mechanisms of calmodulin's functional versatility. [Biochem Cell Biol. 1998]

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Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex.

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