Fig. 4: A high-resolution view of the stem and membrane regions of neurotropic flaviviruses. | Nature Communications

Fig. 4: A high-resolution view of the stem and membrane regions of neurotropic flaviviruses.

From: A unified route for flavivirus structures uncovers essential pocket factors conserved across pathogenic viruses

Fig. 4

a, b A cartoon representation of the a bWNVKUN and b bMVEV structure coloured by domain: E ectodomain 1 (DI, red); E ectodomain 2 (DII, yellow) containing a fusion loop (FL, green) and an N-linked glycan at Asn67 (cyan); E ectodomain 3 (DIII, blue); E membrane domain (purple) consisting of an ‘anchor’ of three perimembrane helices (E-H1, E-H2 and E-H3) and a ‘stem’ of two transmembrane helices (E-T1 and Ea-T2); M membrane domain (magenta) consisting of a perimembrane helix (M-H1) and two transmembrane helices (M-T1 and M-T2). c, d A ribbon representation of local RMSD differences between the structures of c bMVEV and bWNVKUN and d bMVEV and JEV (PDB: 5WSN) where the ribbon diameter is proportional to the RMSD. For bMVEV/bWNVKUN, the RMSD ranges between 0.05 and 2.93 Å with an average of 0.64 Å, whereas bMVEV/JEV has a range of 0.09–4.81 Å and an average of 1.28 Å. e, f A comparison of the density (mesh) for e M-H3 and f E-T2 with the structure of bWNVKUN (orange sticks), bMVEV (blue sticks), and a cryo-EM structure of JEV (green sticks, PDB: 5WSN, EMD-6685). A sequence alignment is displayed below and coloured accordingly. g The density and model of the glycosylation site at Asn154 for bWNVKUN (orange sticks), bMVEV (blue sticks) and JEV (green sticks).

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