Extended Data Fig. 5: Homodimer surface analysis and alignment with E1/E2 heterodimer structure.

a, Surface analysis of the ectodomain part of the E1/E2 homodimeric complex. Display of glycans (left), sequence conservation (consurf⁴⁸; middle), and hydrophobicity (right) of surface exposed amino acids on the ectodomain of the E1/E2 homodimeric complex (8rk0). The orange box highlights a conserved, glycan-free patch exposed on the surface of the complex, which may be involved in the formation of higher oligomeric states of E1/E2 homodimers. The top row is rotated 90 degrees compared to the bottom row. Glycan density is represented in dark grey. b-c, Alignment of E1 and E2 from our modeled structure (8rjj; depicted in blue) with the recently solved E1/E2 monomer structure (7t6x; regions that agree across the two structures are depicted in red and regions that do not agree are depicted in transparent red). Unresolved regions are depicted in grey in the schematics and indicated by broken lines in the structures. The locations of disulfide bonds are numbered and highlighted in yellow.