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The X‐ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi
Author(s) -
Taylor Paul,
Page Antony P,
Kontopidis George,
Husi Holger,
Walkinshaw Malcolm D
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00264-6
Subject(s) - brugia malayi , cyclophilin , cyclophilin a , peptidylprolyl isomerase , biology , nematode , cis trans isomerases , isomerase , biochemistry , filariasis , microbiology and biotechnology , enzyme , immunology , helminths , ecology , gene
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.