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

Paul Taylor, Antony P. Page, George Kontopidis, Holger Husi, Malcolm D. Walkinshaw

Research output: Contribution to journalArticle

23 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)361-366
Number of pages6
JournalFEBS Letters
Issue number2
Publication statusPublished - 1 Mar 1998


Cite this