Crystal structure of cyclophilin from Leishmania donovani at 3.5 Å resolution

Abstract

The crystal structure of cyclophilin from Leishmania donovani has been solved at 3.5 Å resolution. The protein with peptidylprolyl cis-trans isomerase activity is also a receptor for the drug, cyclosporin. The crystal structure of cyclophilin obtained in space group P4₃2₁2 with cell parameters a = b =48.73 Å, c = 140.93 Å and one molecule in the asymmetric unit, was solved by molecular replacement using human cyclophilin A as the search model. The refined low resolution structure (R = 0.218 and /R_free = 0.324) clearly indicates the conservation of the cyclosporin binding-site geometry with respect to human cyclophilin A.