Open AccessStructure of cyclophilin from Leishmania donovani at 1.97 Å resolution
Author(s) -
Venugopal V.,
Sen Banibrata,
Datta Alok K.,
Banerjee Rahul
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106056351
Subject(s) - cypa , cyclophilin , cyclophilin a , leishmania donovani , resolution (logic) , molecular replacement , peptidylprolyl isomerase , crystallography , molecule , biology , protein structure , chemistry , crystal structure , biophysics , stereochemistry , biochemistry , leishmaniasis , microbiology and biotechnology , visceral leishmaniasis , isomerase , enzyme , genetics , organic chemistry , artificial intelligence , computer science , gene
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.