1ctr
From Proteopedia
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DRUG BINDING BY CALMODULIN: CRYSTAL STRUCTURE OF A CALMODULIN-TRIFLUOPERAZINE COMPLEX
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Cavernous malformations of CNS and retina OMIM:[604214], Cerebral cavernous malformations-1 OMIM:[604214], Hyperkeratotic cutaneous capillary-venous malformations associated with cerebral capillary malformations OMIM:[604214], Leukemia, acute T-cell lymphoblastic OMIM:[603025], Leukemia, acute myeloid OMIM:[603025]
About this Structure
1CTR is a Single protein structure of sequence from Homo sapiens with CA and TFP as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 16:25:23 2007
