Adequate treatment of viral infection is a critical issue because of drug resistance. Deepening knowledge of viral lifespan provides new targets for drug design. HSP90 (heat shock protein 90) is one of human proteins which plays a key role in different phases of development of many viral infections including viral entry, nuclear import, transcription, and replication. Riamilovir is an antiviral drug which has passed through all stages of drug development and is used for treatment of influenza, but its chemical structure gives us an opportunity to use it more widely. Riamilovir is from the family of azolazines, anoluge of purine nucleotides and theoretically it can be ligand to the purine protein site of HSP90. Molecular docking is a computational tool for drug evaluation. Molecular docking was performed with the HSP90α molecule (N termination domain) and the results were analyzed. For control, redocking with ligand 8DU (interaction of HSP90α N-domain was confirmed by X-ray crystallography, PDB ID: 5XRB) was carried out. Control docking helped to confirm the presence and location of the active center of the HSP90α N-domain protein. The simulation results show that the most likely interaction of riamilovir with HSP90α N-domain is possible in the same binding pocket as with the control ligand. Based on molecular docking data, riamilovir can be related to HSP90 N-terminal inhibitor.

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