Fig. 5: 1E5 induces two distinct dynamic structures of the G-tetramer. | Nature Communications

Fig. 5: 1E5 induces two distinct dynamic structures of the G-tetramer.

From: A potent Henipavirus cross-neutralizing antibody reveals a dynamic fusion-triggering pattern of the G-tetramer

Fig. 5

a Molecular surface showing two flip-horizontal views of the upper binding loose type of the NiV/1E5 complex. The glycans are marked with gray dotted circles, the two unsolved lower heads are shown in gray, and the other chains are shown in different colors as indicated. b The approximate symmetric structure of the lower binding compact type of the NiV/1E5 complex, represented as a molecular surface. Structural diagram of 1E5 Fabs complexed with the upper two heads of the loose type (c) or the lower two heads of the compact type (d), shown in colored ribbon representation. e The superimposition of GHD-1E5 structures determined by cryo-EM and crystallography. The superimposition of the compact (f) or loose type (g) with the G-tetramer previously reported (PDB ID: 7TXZ/7TY0). Local residue contacts are shown as stick representations in their parent chain colors, and H-bonds are shown as dotted black lines. Heads A, B, C, and D of 7TXZ/7TY0 are colored tan, light medium purple, dark khaki, and light blue, respectively. Heads A, B, C, and D of the loose/compact type are colored teal, violet, cornflower blue, and medium violet red, respectively. 1E5 is colored goldenrod, and nAH1.3 is in salmon. The red dotted line with a bidirectional arrow indicates the offset distance.

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