| 초록 |
As a drug-resistant influenza virus has recently been found from humans, it is urgent and necessary to develop new antiviral drugs. It has been known that the influenza RNA polymerase has a crucial role in viral RNA replication and transcription. It contains three proteins: PA, PB1, and PB2. Recently, the crystal structure of the N-terminal 197 residues of PA was reported. The critical role of the polymerase complex and high sequence conservation indicate that PA is an important target for the design of new anti-influenza drugs. In this study, docking simulation was carried out using dynamic pharmacophore method to take receptor flexibility into account for the analysis of ligand-receptor binding. The aim of this study is to define a pharmacophore model that can be used to design inhibitors of PA. This research will show screening results from drug library, and thereby propose optimal molecular binding interactions. |
