Structure of cyclophilin from Leishmania donovani bound to cyclosporin at 2.6A° resolution: correlation between structure and thermodynamic data
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
Structure of cyclophilin from Leishmania donovani
bound to cyclosporin at 2.6A° resolution: correlation between structure and thermodynamic data
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| Creator |
Venugopal, V
Dutta, Alok K Bhattacharyya, Dhananjay Dasgupta, Dipak Banerjee, Rahul |
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| Subject |
Chemistry
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| Description |
Drug development against Leishmania donovani, the pathogen
that causes visceral leishmaniasis in humans, is currently
an active area of research given the widespread prevalence
of the disease and the emergence of resistant strains. The
immunosuppressive drug cyclosporin is known to have antiparasitic
activity against a variety of pathogens. The receptor
for cyclosporin is the protein cyclophilin, which is a ubiquitous
peptidylprolyl isomerase. The crystal structure of cyclophilin
from L. donovani complexed with cyclosporin has been solved
at 2.6 A ° resolution. The thermodynamic parameters of the
interaction have been determined using spectroscopic and
calorimetric techniques. A detailed effort has been made to
predict the thermodynamic parameters of binding from computations based on the three-dimensional crystal structure. These results were in good agreement with the corresponding experimental values. Furthermore, the structural and biophysical esults have been discussed in the context of leishmanial drug resistance and could also set the stage for the design of potent non-immunosuppressive antileishmanials.
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| Date |
2009
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/963/1/5_acta_crys_2009.pdf
Venugopal, V and Dutta, Alok K and Bhattacharyya, Dhananjay and Dasgupta, Dipak and Banerjee, Rahul (2009) Structure of cyclophilin from Leishmania donovani bound to cyclosporin at 2.6A° resolution: correlation between structure and thermodynamic data. Acta Crystallographica Section D -Biological Crystallography, 65. pp. 1187-1195. |
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| Relation |
http://www.eprints.iicb.res.in/963/
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