Extended Data Fig. 4: Structural comparisons between the receptor-bound and receptor-free VEEV E proteins, overall shape of LDLRAD3-D1 and the low-pH-treated VEEV VLP with the bound LDLRAD3-D1.
From: Structure of Venezuelan equine encephalitis virus with its receptor LDLRAD3
a, Ribbon diagrams showing the LDLRAD3-D1 bound and free VEEV E2 structures. LDLRAD3-D1 and VEEV E2 are shown in ribbons and coloured pink and green, respectively. Upon binding LDLRAD3-D1, conformational changes were observed at residues H96 and H156 of E2. In addition, the E2 loop that involves residues 57-64 becomes ordered in the complex structure owing to the establishment of the salt bridges between R64 of E2 and D54 and D50 of LDLRAD3-D1. b, Ribbon and schematic diagrams showing the elliptical cylinder shape of LDLRAD3-D1. The ribbon of LDLRAD3-D1 is coloured blue through the rainbow spectrum to red (from N to C). c, Cryo-EM images of the low pH treated VEEV VLP complexed with LDLRAD3-D1 showing the aggregated particles, which is an indication for the exposure of the fusion loop.
