Figure 9.

Comparison of the DI-DII hinge angle of the crystal structures of rE protein with the cryo-EM structures of virus E protein.

1. Superposition of the crystal structures of rE and the subnanometer resolution cryo-EM structures of virus E proteins showed that the hinge angles of rE proteins are variable whereas those on the virus surface are largely conserved. DI of these structures was superimposed using ‘LSQ superpose’ in COOT (Emsley et al, 2010).
2. Zoom-in view of the part of the HMAb 1F4 epitope that consists of the kl loop (represented as sticks) in the DI-II hinge region. The kl loops from the viruses (left) showed conserved conformation whereas those from the rE proteins (right) showed varying conformations. Residue 274, which is critical for HMAb 1F4 binding (De Alwis et al, 2012), is shown as a sphere.