Dimerization of Hepatitis E Virus Capsid Protein E2s Domain Is Essential for Virus–Host Interaction
Figure 1
(A) Ribbon diagram of the subunit of the E2s dimer, side view. (B) Top view of the subunit of E2s dimer showing the cavity. β-strands and random coils/turns are depicted in red and green respectively. N- and C-termini are labeled. The dimerization interface and groove region are labeled. (C) The E2s dimer. Subunit A is shown in yellow, subunit B in red. Dimeric interface residues from both subunits are shown in ball-and-stick representation. Notably, the asymmetric unit consists of one subunit of the dimer. This dimer is generated by crystallographic symmetry. These figures were prepared by using Molscript and Raster3D [32],[33]. (D) Close-up view of the dimer interface. Key residues involved in the dimerization are labeled. This figure was prepared using PyMol [34].