Fig. 2: Overall structure of the NiV L-P complexes from both NiV-M and NiV-B. | Nature Communications

Fig. 2: Overall structure of the NiV L-P complexes from both NiV-M and NiV-B.

From: Cryo-EM structures of Nipah virus polymerases and high-throughput RdRp assay development enable anti-NiV drug discovery

Fig. 2: Overall structure of the NiV L-P complexes from both NiV-M and NiV-B.

a Domain organization of NiV L and P proteins. L contains the following five domains: RdRp domain (marine), PRNTase domain (lime green), CD (gray), MT domain (gray), and CTD (gray). Residues in the active site of the RdRp (GDN) and the PRNTase domain (GXXT and HR) are indicated. Locations of six conserved regions (CR-I to CR-VI) are highlighted. P contains an N-terminal Domain (NTD, in gray), an oligomerization domain (OD, in orange, brown, light pink, or dark pink), and a C-terminal Domain (CTD, in dark pink). At the C terminus, P has an X domain (XD, in dark pink). The NiV proteins P interacts with are indicated on the top. Predicted phosphorylation sites of P are shown below. Cryo-EM density map fitted with the model for FL NiV-M L-P (b), TR NiV-M L-P (c), and TR NiV-B L-P (d) and another view of the models with a 180° turn. In b, c, d, individual domains are colored as depicted in (a), and the right panels are views with the NTP entry channel facing outward, defined as the front view in this study.

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