1a58 | pdb_00001a58

CYCLOPHILIN FROM BRUGIA MALAYI

spinqualitylabelsall models 1a58, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1a58 is a 1 chain structure with sequence from Bruma. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: CYCLOPHILIN (BRUMA) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cyclophilin

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