Fig. 3: Structural comparison of VP8*B crystal structure with AlphaFold2 prediction. | Communications Biology

Fig. 3: Structural comparison of VP8*B crystal structure with AlphaFold2 prediction.

From: Novel fold of rotavirus glycan-binding domain predicted by AlphaFold2 and determined by X-ray crystallography

Fig. 3

a, b Superimposition of chain A and B of VP8*B in the crystallographic asymmetric unit with the AlphaFold2-predicted model. Crystal structure of RVP8*B with chains A and B colored in blue and purple, respectively. The resides 72–202 of the highest-ranked AlphaFold model is shown as a yellow ribbon diagram. The N- and C-termini of VP8*B are labeled. c The close-up view of the region in the black box in (b). The superimposed models are shown side-by-side for clarity. d Example of structural difference between the AlphaFold2 model (yellow) and crystal structure (chain A, blue). The hydrogen bonds are shown as black dashed lines. The experimental 2Fo-Fc map of the residues is shown as gray mesh.

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