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. Author manuscript; available in PMC: 2017 Dec 1.
Published in final edited form as: Hepatology. 2016 Oct 28;64(6):1922–1933. doi: 10.1002/hep.28850

Figure 2. Structure of the HC84.26.5D–E2434–446 complex.

Figure 2

(A) Ribbon diagram of the HC84.26.5D–E2434–446 complex (side view). VL, green; VH, cyan; E2434–446, orange. VLCDR loops are labeled L1–L3; VHCDR loops are labeled H1–H3. The side chains of epitope residues Trp437, Phe442, Tyr443, and Lys446 are drawn in stick representation. (B) Conformation of the E2434–446 epitope bound to HC84.26.5D and in unbound E2 core protein. The E2434–446 epitope from the complex with HC84.26.5D (orange) was superposed onto E2434–446 from the complex with HC84.1 (yellow) (Protein Data Bank accession code 4JZN) (16), and onto E2434–446 from the structure of the E2 core glycoprotein (wheat) (4MWF) (9). The E2434–446 epitopes were superposed through residues 437–442. The N- and C-termini are labeled. The epitopes are in the same overall orientation as in (A).