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. Author manuscript; available in PMC: 2019 Oct 2.
Published in final edited form as: Structure. 2018 Aug 9;26(10):1314–1326.e4. doi: 10.1016/j.str.2018.06.012

Figure 3. The e13 and e21 Epitopes Overlap with the HBV Capsid Dimer-dimer Interface.

Figure 3.

(A) Overlaid structure of the rHBcAg-scFv e13 complex with a rHBcAgc dimer-dimer interface (PDB ID = 1QGT). (B) Overlaid structure of the rHBcAg-Fab e21 complex with a rHBcAgc dimer-dimer interface. The two interacting rHBcAg monomers from individual core dimers are shown as blue and gold ribbons. For clarity, the remaining rHBcAg monomers of each dimer are not shown. The variable chains of scFv e13 and Fab e21 are shown as pink semi-transparent surfaces. The rHBcAgc dimer-dimer interfaces are indicated with arrows. (C) Locations of scFv e13 CDRs with respect to the rHBcAgc dimer-dimer interface. (D) Locations of Fab e21 CDRs with respect to the rHBcAgc dimer-dimer interface. The variable chains of scFv e13 and Fab e21 are shown as pink and yellow ribbons, respectively. The heavy chain CDRs are shown in orange and numbered from H1-H3, and the light chain CDRs are shown in green and numbered from L1-L3. The rHBcAgc dimer-dimer interfaces, as calculated with FADE, are shown as blue semi-transparent surfaces.