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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 1. Crystal Structures of Immune Complexes.

Figure 1.

(A) rHBcAgd-scFv e13 at 3.33 Å, (B) rHBeAgd-scFv e13 at 2.38 Å, and (C) rHBcAgd-Fab e21 at 3.15 Å resolution. The rHBcAg and rHBeAg monomers are shown as gold and blue ribbons. Surface representations of the variable heavy chain fragments (VH) and variable light chain fragments (VL) are shown in pink and gray, respectively. The N-terminal 10 amino acid pro-peptide (PP) in rHBeAg is shown in magenta. (D) Overlaid structures of scFv e13, Fab e21 and Fab me6 bound to rHBeAg (for clarity only a single chain is shown for the rHBeAg although the protein is dimeric). rHBeAg is represented as a ribbon where the alpha-helical regions are color-coded (DiMattia et al., 2013). The panel below shows the corresponding amino acid ranges for each region. α4 is divided into two helices, α4a and α4b, separated by a kink at residues V99-G104. Only the variable chains of the antibody fragments are shown as surfaces (scFv e13 in pink, Fab e21 in yellow, and Mab me6 in blue). See also Figure S1, Figure S3, Figure S5 and Figure S6.