Structure of cyclophilin from Leishmania donovani at 1.97 angstrom resolution
Metadata of CSIR Papers
View Archive Info| Field | Value | |
| Title |
Structure of cyclophilin from Leishmania donovani at 1.97 angstrom resolution
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| Creator |
Venugopal, V
Sen, B Datta, AK Banerjee, R |
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| Subject |
Biochemical Research Methods; Biochemistry & Molecular Biology; Biophysics; Crystallography
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| Description |
The crystal structure of cyclophilin from Leishmania donovani (LdCyp) has been determined and refined at 1.97 angstrom 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.
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| Publisher |
BLACKWELL PUBLISHINGOXFORD9600 GARSINGTON RD, OXFORD OX4 2DQ, OXON, ENGLAND
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| Date |
2011-09-20T12:12:40Z
2011-09-20T12:12:40Z 2007 |
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| Type |
Article
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| Identifier |
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
1744-3091 http://hdl.handle.net/123456789/14373 |
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| Language |
English
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