Structure of cyclophilin from Leishmania donovani at 1.97 Å resolution

Abstract

The crystal structure of cyclophilin from Leishmania donovani (LdCyp) has been determined and refined at 1.97 Å resolution to a crystallographic R factor of 0.178 (R free = 0.197). The structure was solved by molecular replacement using cyclophilin from Trypanosoma cruzi as the search model. LdCyp exhibits complete structural conservation of the cyclosporin-binding site with respect to the homologous human protein, as anticipated from LdCyp-cyclosporin binding studies. Comparisons with other cyclophilins show deviations primarily in the loop regions. The solvent structure encompassing the molecule has also been analyzed in some detail. © International Union of Crystallography 2007.