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1: Biochemistry. 2000 Jan 25;39(3):592-8.Click here to read Links

Crystal structure of the complex of brugia malayi cyclophilin and cyclosporin A.

Ellis PJ, Carlow CK, Ma D, Kuhn P.

Stanford Synchrotron Radiation Laboratory, SLAC, P.O. Box 4249, Bin 69, Stanford University, Stanford, California 94309, USA.

The resistance of the human parasite Brugia malayi to the antiparasitic activity of cyclosporin A (CsA) may arise from the presence of cyclophilins with relatively low affinity for the drug. The structure of the complex of B. malayi cyclophilin (BmCYP-1) and CsA, with eight independent copies in the asymmetric unit, has been determined at a resolution of 2.7 A. The low affinity of BmCYP-1 for CsA arises from incomplete preorganization of the binding site so that the formation of a hydrogen bond between His132 of BmCYP-1 and N-methylleucine 9 of CsA is associated with a shift in the backbone of approximately 1 A in this region.

PMID: 10642184 [PubMed - indexed for MEDLINE]

Structures reported by this article

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