The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi.
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
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Structural Biochemistry Group, The University of Edinburgh, UK.
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Kontopidis
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Husi
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Walkinshaw
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D000595:Amino Acid Sequence; D000818:Animals; D017178:Brugia malayi / Q000201:enzymology*; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019696:Peptidylprolyl Isomerase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013698:Templates, Genetic
D011993:Recombinant Fusion Proteins; D019696:Peptidylprolyl Isomerase