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Structure of Cyclophilin from Leishmania donovani at 1.97A° Resolution

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Title Structure of Cyclophilin from Leishmania donovani
at 1.97A° Resolution
 
Creator Venugopal, V
Sen, Banibrata
Datta, Alok K
Banerjee, Rahul
 
Subject Structural Biology & Bioinformatics
 
Description 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 (Rfree = 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.
 
Date 2007
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/1043/1/ACTA_CRYSTALLOGRAPHICA_SECTION_F%2DSTRUCTURAL_BIOLOGY_AND_CRYSTALLIZATION_COMMUNICATIONS__63__60%2D64;2007[114].pdf
Venugopal, V and Sen, Banibrata and Datta, Alok K and Banerjee, Rahul (2007) Structure of Cyclophilin from Leishmania donovani at 1.97A° Resolution. Acta Crystallographica Section F Structural Biology and Crystallization Communications, F63. pp. 60-64.
 
Relation http://dx.doi.org/10.1107/S1744309106056351
http://www.eprints.iicb.res.in/1043/