Upendra Yadav C/O Dr. Vandana Rai Human Molecular Genetics Laboratory, Department of Biotechnology, VBS Purvanchal University, Jaunpur (UP)-222001, India
Abstract: This study evaluates the frequency of 5, 10-methylenetetrahydrofolate reductase (MTHFR) C677T mutation in eastern Uttar Pradesh population (UP). PCR-RFLP method was used for the detection of C677T mutation. In total 139 subjects were analyzed for the MTHFR C677T polymorphism. Genotype frequencies of CC, CT and TT were found to be 0.928, 0.065 and 0.007 respectively. The frequency of T allele was 0.039.
Abstract: The present study was aimed to analyze methionine synthase reductase (MTRR) A66G polymorphism in Uttar Pradesh (UP) population and PCR-RFLP method was used for the mutation analysis. Total 104 samples were analyzed and AA genotype was found in 10 individuals, AG genotype in 67 individuals and GG in 27 individuals. The frequencies of AA, AG and GG genotypes in the present study were also assessed with the expected distribution (i.e. Hardy-Weinberg equilibrium) by using χ2 test. The genotype frequencies of AA, AG and GG were 0.096, 0.644 and 0.259, respectively. Allelic frequencies of A and G were 0.418 and 0.581. It was reflected from the results of the present study that the percentage of heterozygous genotype (AG) is highest in the target population.
Abstract: In present study an in silico attempt was made to verify earlier wet lab reports of less affinity of A222V mutant MTHFR with its cofactor FAD by docking. Docking can assist in predicting protein-protein and protein-ligand interactions, and evaluating affinity of complexes. Docking was performed using wild and mutant MTHFR as receptor and FAD as ligand by Hex 5.1 software. 656 long amino acid sequence of MTHFR was extracted from Swissprot and submitted to ESyPred for structure prediction. ESyPred predicted wild as well as mutant MTHFR structure of only 292 amino acids long (i.e. of catalytic domain only). Docking between wild MTHFR-FAD and 677T mutant MTHFR-FAD were performed separately. The E-total (energy) was -375.98 in case of 222A MTHFR-FAD docking and -385.65 in case of 222V MTHFR-FAD docking. Stability of docked complex increased with decrease in energy value. Thus, in silico approach proved that the enzymatic activity of 222V mutant MTHFR is less and reduced due to lower affinity to FAD.
