| 초록 |
The RNA polymerase of influenza virus is comprised of three subunits, PB1, PB2, and PA. The interface between PB1 and PB2 subunits can be a promising target for drug design, not only because it is essential for the polymerase activity but also because it is completely conserved among avian and human influenza viruses. In this work, we aimed to reveal detailed interaction sites on the PB1-PB2 interface. From 40-ns molecular dynamics simulation and subsequent calculation of pair interaction energy, the binding hot spots in the PB1-PB2 complex were determined, and the conformational changes of both PB1 and PB2 subunits in the dynamic interaction process were described. Eight out of 35 residues on PB2 accounts for approximately 60% of the binding energy. Furthermore, the majority of the electrostatic interaction energy is mainly contributed by Glu2, Arg3, Glu6, Arg17, and Lys32, suggesting that these regions are important parts of the polymerase complex. |
