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.
Taylor, P., Page, A. P., Kontopidis, G., Husi, H., & Walkinshaw, M. D. (1998). The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi. FEBS Letters, 425(2), 361-366. https://doi.org/10.1016/S0014-5793(98)00264-6