Fig. 1 | Nature Communications

Fig. 1

From: Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope

Fig. 1

Crystal structures of natively glycosylated HIV-1 Env trimers complexed with BG18. a Cartoon representation of the 3.8 Å structure of BG505 Env (gp120, light gray; gp41, dark gray) in complex with BG18 (blue) and 35O22 (orange) Fabs. Ordered, native high-mannose glycans (cyan) are represented as sticks, and complex-type glycans (salmon) are shown as spheres. b 4.9 Å structure of B41 Env bound to BG18 (blue) and 35O22 (orange). Glycans shown as cyan spheres. c 6.7 Å structure of BG505 Env bound to BG18 (blue) and IOMA (green) Fabs. Glycans were not modeled due to the limited resolution. d Close-up of the BG18 binding site (VH in dark blue, VL in light blue superimposed on the final 2Fo−Fcalc electron density map contoured at 1.2σ) on the surface of gp120 (gray) from the BG18-BG505-35O22 structure. Ordered glycans (cyan) near the BG18 binding site are represented as sticks

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