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1ctr

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1ctr, resolution 2.45Å ()
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

DRUG BINDING BY CALMODULIN: CRYSTAL STRUCTURE OF A CALMODULIN-TRIFLUOPERAZINE COMPLEX

Publication Abstract from PubMed

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.

Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex., Cook WJ, Walter LJ, Walter MR, Biochemistry. 1994 Dec 27;33(51):15259-65. PMID:7803388

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1ctr is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Cook WJ, Walter LJ, Walter MR. Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex. Biochemistry. 1994 Dec 27;33(51):15259-65. PMID:7803388

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