Fig. 5. Spatial organization and curvature are critical determinants of NgR1–reovirus complex stability. Models of NgR1 binding interfaces with reovirus heterohexamers reconstituted on a planar support or within the curved virus capsid. The concave NgR1 interface binds more strongly to individual heterohexamers compared to densely packed self-assembled structures (lower koff), however the multimeric heterohexamer arrangement promotes a higher association rate (higher kon). The local curvature of the viral capsid in reovirus native topology allows for a greater accessibility of the NgR1-binding groove between σ3 subunits from adjacent heterohexamers, which plays a key role in the stability of the complex (lower koff). Created with BioRender.com.
