Structural highlights
Function
[CYP1_BRUMA] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Taylor P, Page AP, Kontopidis G, Husi H, Walkinshaw MD. The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi. FEBS Lett. 1998 Mar 27;425(2):361-6. PMID:9559680
