1A58
CYCLOPHILIN FROM BRUGIA MALAYI
Summary for 1A58
Entry DOI | 10.2210/pdb1a58/pdb |
Descriptor | CYCLOPHILIN (2 entities in total) |
Functional Keywords | isomerase, ppiase |
Biological source | Brugia malayi |
Total number of polymer chains | 1 |
Total formula weight | 19504.42 |
Authors | Taylor, P.,Page, A.P.,Kontopidis, G.,Husi, H.,Walkinshaw, M.D. (deposition date: 1998-02-20, release date: 1998-05-27, Last modification date: 2024-02-07) |
Primary citation | Taylor, P.,Page, A.P.,Kontopidis, G.,Husi, H.,Walkinshaw, M.D. The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi. FEBS Lett., 425:361-366, 1998 Cited by PubMed Abstract: 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. PubMed: 9559680DOI: 10.1016/S0014-5793(98)00264-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
Download full validation report
