3EOV

Crystal structure of cyclophilin from Leishmania donovani ligated with cyclosporin A

Summary for 3EOV

• Entry DOI: 10.2210/pdb3eov/pdb
• Related: 1BCK 1C5F 1CSA 1CWA 1CWB 1CWC 1CWF 1CWH 1CWI 1CWJ 1CWK 1CWL 1CWM 1CWO 1CYA 1CYB 1CYN 1IKF 1M63 1MF8 1MIK 1QNG 1QNH 1XQ7 2ESL 2HAQ 2OJU 2POY 2RMA 2RMB 2RMC 2WFJ 2X2C 2X7K 2Z6W 3BO7 3CYS
• Related PRD ID: PRD_000142
• Descriptor: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, CYCLOSPORIN A (3 entities in total)
• Functional Keywords: isomerase-immunosuppressant complex, cyclophilin-cyclosporin complex, cyclosporin a, immunosuppressant, cyclophilin, isomerase/immunosuppressant
• Biological source: LEISHMANIA DONOVANI; More
• Total number of polymer chains: 4
• Total formula weight: 40622.33

Authors

Venugopal, V.,Dasgupta, D.,Datta, A.K.,Banerjee, R. (deposition date: 2008-09-29, release date: 2008-11-11, Last modification date: 2023-11-15)

Primary citation

Venugopal, V.,Datta, A.K.,Bhattacharyya, D.,Dasgupta, D.,Banerjee, R.
Structure of Cyclophilin from Leishmania Donovani Bound to Cyclosporin at 2.6 A Resolution: Correlation between Structure and Thermodynamic Data.
Acta Crystallogr.,Sect.D, 65:1187-, 2009

PubMed Abstract: Drug development against Leishmania donovani, the pathogen that causes visceral leishmaniasis in humans, is currently an active area of research given the widespread prevalence of the disease and the emergence of resistant strains. The immunosuppressive drug cyclosporin is known to have antiparasitic activity against a variety of pathogens. The receptor for cyclosporin is the protein cyclophilin, which is a ubiquitous peptidylprolyl isomerase. The crystal structure of cyclophilin from L. donovani complexed with cyclosporin has been solved at 2.6 A resolution. The thermodynamic parameters of the interaction have been determined using spectroscopic and calorimetric techniques. A detailed effort has been made to predict the thermodynamic parameters of binding from computations based on the three-dimensional crystal structure. These results were in good agreement with the corresponding experimental values. Furthermore, the structural and biophysical results have been discussed in the context of leishmanial drug resistance and could also set the stage for the design of potent non-immunosuppressive antileishmanials.

PubMed: 19923714
DOI: 10.1107/S0907444909034234

Experimental method

X-RAY DIFFRACTION (2.6 Å)