Structure of cyclophilin from Leishmania donovani at 1.97 A resolution.
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.
Venugopal
V
V
Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, Sector 1, Block AF, Bidhan Nagar, Kolkata 700 064, India.
Sen
Banibrata
B
Datta
Alok K
AK
Banerjee
Rahul
R
D000818:Animals; D001665:Binding Sites; D018360:Crystallography, X-Ray; D021983:Cyclophilins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D007893:Leishmania donovani / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D014867:Water / Q000737:chemistry
D011994:Recombinant Proteins; D014867:Water; D021983:Cyclophilins