Fig. 5: Inhibition activity of suramin against NiV L-P complex.
From: Cryo-EM structure of Nipah virus L-P polymerase complex
a Inhibition activity of suramin against NiV L-P complex at the enzymatic level. Data are representative of two independent experiments using different protein preparations, and both experiments showed similar results. b Inhibition activity of suramin against NiV L-P complex in replicon cell. The suramin displayed obvious inhibitory effects on NiV polymerase in vitro and in vivo. Each point represents mean values ± s.d. (error bar) of three independent experiments using different cell preparations. c Molecular docking of suramin in NiV L protein. The structure was shown as surface and colored by domains. Suramin could bind at the NTP entry channel and prevent the substrates from entering the active site to inhibit the polymerase activity. d The interactions between NiV L protein and suramin in the docking structures. Several polar residues could form hydrogen bonds, π-π, and π-cation interactions with the suramin. The hydrogen bonds were indicated by dashed yellow lines and the π-π and π-cation interactions were indicated by dashed black lines. Source data are provided as a Source Data file.
