Fig. 2
From: Glycan recognition in globally dominant human rotaviruses
VP8* structure of a neonatal human rotavirus strain P[6] RV3 and structural comparison with VP8*s of other HRVs in complex with HBGAs. a Ribbon representation of the P[6] RV3 VP8* structure displays a galectin-like fold with the two twisted β-sheets in yellow and green, respectively. The β-hairpin and the C-terminal α-helix and are colored in orange and purple, respectively. b Structural superposition of P[6] VP8* (gray) with HRV P[14] VP8* (light blue) in complex with A-type HBGA (PDB ID: 4DRV) and HRV P[11] VP8* (tan) in complex with LNT (PDB ID: 4YFZ). The width of the cleft between the β-sheets in P[6] and P[11] VP8*s is wider than that in P[14] VP8*, as indicated by red and black arrows, respectively. The glycans bound on VP8* are represented with sticks. Close-up views of the A-type HBGA (c) and LNT (d) binding sites show the amino acid changes in P[6] VP8* disallow the glycan binding at these sites. The interacting residues are shown in stick model and labeled. The proteins are colored as in b
