CYCLOPHILIN FROM BRUGIA MALAYI
[CYP1_BRUMA] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Publication Abstract from PubMed
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.
The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi.,Taylor P, Page AP, Kontopidis G, Husi H, Walkinshaw MD FEBS Lett. 1998 Mar 27;425(2):361-6. PMID:9559680
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.