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The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi
P Taylor1, A P Page, G Kontopidis
1Structural Biochemistry Group, The University of Edinburgh, UK.
Abstract:
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.
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