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

P Taylor, A P Page, G Kontopidis, H Husi, M D Walkinshaw

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Pages (from-to)361-6
Number of pages6
JournalFEBS Letters
Volume425
Issue number2
Publication statusPublished - 1998

Fingerprint

Dive into the research topics of 'The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi'. Together they form a unique fingerprint.

Cite this