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Updated: Jul 17, 2026

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach
Published on: June 23, 2026
Structure of cyclophilin from Leishmania donovani at 1.97 A resolution
V Venugopal1, Banibrata Sen, Alok K Datta
1Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, Sector 1, Block AF, Bidhan Nagar, Kolkata 700 064, India.
Abstract:
The crystal structure of cyclophilin from Leishmania donovani (LdCyp) has been determined and refined at 1.97 A 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.

