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Posters: J Proteomics Bioinform
Malaria is a major public health concern and its parasites have developed resistance to the commonly available drug. So, now days it?s a major concern to find out new target for drug therapy. Plasmodium falciparum 3D7 is one of the strains of plasmodium species also lacks in functional TCA cycle and solely dependent on glycolysis for its energy supply like other plasmodium species.. Although parasite enzymes have been considered as potential antimalarial drug targets, little is known about their structural biology. Here the tertiary structure of triose phosphate isomerase of Plasmodium falciparum 3D7 was determined by means of homology modeling through multiple alighment followed by intensive optimization and validation. The modeling was done by SWISS MODEL WORK SPACE. The obtained models was verified with the structure validation programs like ,PROCHECK, Verify 3D and QMEAN for reliability. The verify 3D value 0.69 indicates that the environment profile of the model is good . Self Optimized Prediction Method with Alignment or SOPMA is employed for calculating the secondary structural features of triose phosphate isomerase The secondary structure indicates the predicted 3D structure of triose phosphate isomerase of Plasmodium falciparum 3D7 contains 48.37% alpha helix ,29.27% random coil and 16.67% extended strand. Active site determination through CASTp suggests that this protein can acts as potential drug target. However, these will further be tested by wet lab studies for a targeted vaccine design against Plasmodium falciparum 3D7.