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. Author manuscript; available in PMC: 2021 Feb 23.
Published in final edited form as: Vaccine. 2012 Oct 26;31(2):417–424. doi: 10.1016/j.vaccine.2012.10.073

Figure 6.

Figure 6

Antigenic structure and dimeric interface of the P-domain. (A) Surface presentation of a HEV dimer, in which the P-, M-, and S-domain are colored in grey, slate blue, and light pink, respectively. The antibody-binding amino acids identified by mutagenesis are colored in red. They overlap with HEP224 binding-site (green) at residue S487 (yellow) and with 8C11 binding-site (magenta) at residue D496 (colored in brown). (B) Surface potential representation of PORF2 mononer to show the dimeric contacting interface at the P-domain. The blue region is positively charged while red region is negatively charge and white region is non-polar. The amino acids of ball-and-stick mode label the residues critical to dimer formation.