computational elucidation of interface site interaction studies of ldiscsglu409&glu347 and ldiscuarg49&lys149 of the iron-sulphur cluster assembly proteins: an implication for designing of novel therapeutic strategies

Leishmaniasis is a rare tropical disease that causes severe loss of life and this causes a significant burden to all developing countries, including indian subcontinents. a regulatory system occurs inside the parasitic organism that contains iron-containing enzymes (ldiscu and ldiscs) for survival activities. here we generated the homology model of these two proteins and the generated model and selection of the best model structure validated by the ramachandran plot is found to be 98.0% residues are in the energetically most favoured region and ldiscs has 94.4% residues in the favoured area, (4.2%) residues in the allowed region, and 1.4 % (6) residues in the disallowed region. the result suggested that the interacting amino acids involved in the interaction between two proteins are (ldiscs protein) are gln429, leu421, ser422, val346, glu385, cys345, ser34, arg313, arg321, asn386, leu424 and trp425 with arg32, lys142, lys147, ser148, lys149, ser151, glu53, gly55, thr46 and ala134 amino acids of ldiscu protein. salt bridge interaction analysis also revealed the interacting amino acids of ldiscs are glu409 with arg49 of ldiscu (4.31 å) and ldiscs of glu347 with lys149 of ldiscu (4.80 å) have strong interaction between assembly essential proteins for the successful transfer of ions. the md simulations studies suggested that these two interacting proteins forms the stable complex. the pca analysis result suggests that the pc1, pc2 and pc3 for ldiscs accounted for 38.07%, 7.89% and 8.57% of the variance, respectively, whereas the other pcs each contributed less than 8% except for specific instances such as pc3 in ldiscs, which contributed 8.57%.