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Figure 1 | Veterinary Research

Figure 1

From: Structural analysis and insertion study reveal the ideal sites for surface displaying foreign peptides on a betanodavirus-like particle

Figure 1

Three dimensional structure of OGNNV VLP (RBS). A The outside view of the RBS capsid. The red triangle demonstrates an asymmetry unit and the digits of 5, 3 and 2 show the position of the five, three and twofold axis. B The cut-way view shows the inward structure of the RBS capsid. The color bar shows the color scheme in the radius. The contour of A and B is 3.5. C The left one shows the surface map of RBS with the contour of 1.2. The color scheme is the same as A and B. It demonstrates that there are 60 protrusions outside the capsid shell, and the zoom in view (low passed to 8 Å) shows there are three linker loops that link the protrusion to the capsid. The red circles demonstrate the location of the residue Ala220. The contour of the right one is 0.6. D, E are the outside and inside view of an asymmetry unit density map superimposed by their models, respectively. The density maps are in gray, and the ribbon models of VPa, VPb and VPc are colored in golden, cornflower blue and purple, respectively. The outside view shows that the Ala220 residue (red circle) is at the surface of the capsid, while the inside view shows that all the residues of the N-terminal of the VPa and VPb (blue circles) are inside the capsid. For the VPc, 17 more residues which belong to the N domain form a loop (black arrow) across the VPb. F The features of a fragment of helix (left) and loop (right) at current resolution obviously demonstrate the big side chain densities. The models in golden color are superimposed in the density map (gray mesh). The contour of the map shown here is 3.2.

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