Mechanistic insights into Zika virus NS3 helicase inhibition by Epigallocatechin-3-gallate: Supplementary Files

Deepak Kumar; Nitin Sharma; Murali Aarthy; Sanjeev Singh; Rajanish Giri

In a further study, EGCG was docked at RNA binding cavity ( Figure 2 ) of NS3 helicase. Interestingly, EGCG was showing almost similar docking score (-7.762) as observed against ATPase site (table 1). In Figure 2B and 2C, EGCG was found to interact with RNA binding site where residues ASP 410, MET 414, LEU 430 and THR 225 were showing H-bonding with EGCG and residues LYS 431, PHE 289 were found to show Pication and Pi-Pi stacking interactions respectively. From figure 2D , it can be interpreted that EGCG is binding at the entry site of the RNA molecule. Thus, it could probably interfere with helicase activity also. The residues involved in interaction with EGCG, have been shown to play an essential role in binding with RNA and further complete helicase function (21) . From our docking studies, it is clear that EGCG has the potential to bind at both sites on NS3 helicase with significant interactions.