Journal of Proteomics & Bioinformatics
Open Access
ISSN: 0974-276X
ISSN: 0974-276X
Pradeep Kumar M, Kranthi Raj.K, D. Ramachandran, Pavan Kumar MNS, Radha Vaddavalli and P. Jhansi lakshmi
A three dimensional model was developed for Plasmodium falciparum Farnesyltransferase (PfFT) that has not been solved empirically by X-ray crystallography or NMR. Homology modeling was used for the structure predic tion using farnesyltransferase protein 2ZIR 2.4 Å (Rat), and 1JCQ 2.3 Å (Human) a moderate-resolution X-ray crystallography structures . The former showed 36% and the latter, 35% sequence identity with the target PfFT protein. The 3D-model was generated by using modeler in Discovery studio 2.5. The energy refinement was also been carried out in the modeler protocol. The validation study showed 88.2% of the residues (750) to be in the favourable region. In addition binding affinities of some inhibitors were investigated against the modeled protein using GOLD. The results showed that Arg-551, Tyr-824, Tyr-600 were found to be among the interacting residues of PfFT with many of the inhibitors. Our findings could be helpful for the design of new and more potent PfFT inhibitors. .