1C5F

CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A

Replaces:  1QTL

Summary for 1C5F

• Entry DOI: 10.2210/pdb1c5f/pdb
• Related: 1BCK 1CSA 1CWA 1CWB 1CWC 1CWF 1CWH 1CWI 1CWJ 1CWK 1CWL 1CWM 1CWO 1CYA 1CYB 1CYN 1IKF 1M63 1MF8 1MIK 1QNG 1QNH 1XQ7 2ESL 2OJU 2POY 2RMA 2RMB 2RMC 2WFJ 2X2C 2X7K 2Z6W 3BO7 3CYS 3EOV
• Related PRD ID: PRD_000142
• Descriptor: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE 1, CYCLOSPORIN A (3 entities in total)
• Functional Keywords: isomerase-immunosuppressant complex, cyclophilin-cyclosporin complex, cyclosporin a, immunosuppressant, cyclophilin, isomerase/immunosuppressant
• Biological source: BRUGIA MALAYI; More
• Total number of polymer chains: 16
• Total formula weight: 165800.34

Authors

Ellis, P.J.,Carlow, C.K.S.,Ma, D.,Kuhn, P. (deposition date: 1999-11-22, release date: 1999-12-03, Last modification date: 2023-12-27)

Primary citation

Ellis, P.J.,Carlow, C.K.,Ma, D.,Kuhn, P.
Crystal Structure of the Complex of Brugia Malayi Cyclophilin and Cyclosporin A.
Biochemistry, 39:592-, 2000

PubMed Abstract: The resistance of the human parasite Brugia malayi to the antiparasitic activity of cyclosporin A (CsA) may arise from the presence of cyclophilins with relatively low affinity for the drug. The structure of the complex of B. malayi cyclophilin (BmCYP-1) and CsA, with eight independent copies in the asymmetric unit, has been determined at a resolution of 2.7 A. The low affinity of BmCYP-1 for CsA arises from incomplete preorganization of the binding site so that the formation of a hydrogen bond between His132 of BmCYP-1 and N-methylleucine 9 of CsA is associated with a shift in the backbone of approximately 1 A in this region.

PubMed: 10642184
DOI: 10.1021/BI991730Q

Experimental method

X-RAY DIFFRACTION (2.47 Å)