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1: FEBS Lett. 1998 Mar 27;425(2):361-6.Click here to read Links

The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi.

Taylor P, Page AP, Kontopidis G, Husi H, Walkinshaw MD.

Structural Biochemistry Group, The University of Edinburgh, UK.

A structure of residues 1-177 of the cyclophilin domain of a large divergent cyclophilin from the filarial nematode parasite Brugia malayi has been crystallised and solved in two different crystal forms. The active site has a similar structure to that of human cyclophilin A. Two of the 13 residues important in forming the human cyclophilin A/cyclosporin A complex are altered in the B. malayi cyclophilin and explain the relatively poor inhibition of peptidyl prolyl isomerase activity by cyclosporin A.

PMID: 9559680 [PubMed - indexed for MEDLINE]

Structures reported by this article