Fig. 4: Interactions and binding configuration between the L protein and four P protomers in FL NiV-M L-P. | Nature Communications

Fig. 4: Interactions and binding configuration between the L protein and four P protomers in FL NiV-M L-P.

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

Fig. 4: Interactions and binding configuration between the L protein and four P protomers in FL NiV-M L-P.

a A front view of the FL NiV-M L-P is shown in the cartoon and colored as depicted in Fig. 2. Four P protomers are labeled by P1, P2, P3, and P4. The P protein fragments extend from the C-terminal of P-OD and are highlighted by a thicker loop radius. G831 in the GDN is shown as magenta spheres. In the dashed line box on the top, four P protomers are shown side by side and in superposition. The P-OD part is nearly identical, whereas the structures downstream vary depending on their binding sites on the L protein. P-CTD is shown, which is assigned to P4. Two side views are shown below to highlight the locations of the six L-P binding interfaces. The NTP entry and template entry are indicated. b Magnified view of the interactions between L and P proteins at the six interfaces. Structural elements, including the RdRp and P protomers and residues that participate in the interactions, are indicated. The potential hydrogen bonds and electrostatic interactions are depicted as dashed lines, with oxygen and nitrogen atoms shown in red and blue, respectively.

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