1CTR

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

Summary for 1CTR

• Entry DOI: 10.2210/pdb1ctr/pdb
• Descriptor: CALMODULIN, CALCIUM ION, 10-[3-(4-METHYL-PIPERAZIN-1-YL)-PROPYL]-2-TRIFLUOROMETHYL-10H-PHENOTHIAZINE (3 entities in total)
• Functional Keywords: calcium-binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton, spindle: P62158
• Total number of polymer chains: 1
• Total formula weight: 17289.16

Authors

Cook, W.J.,Walter, L.J.,Walter, M.R. (deposition date: 1994-09-21, release date: 1994-12-20, Last modification date: 2024-02-07)

Primary citation

Cook, W.J.,Walter, L.J.,Walter, M.R.
Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex.
Biochemistry, 33:15259-15265, 1994

PubMed Abstract: 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.

PubMed: 7803388
DOI: 10.1021/bi00255a006

Experimental method

X-RAY DIFFRACTION (2.45 Å)