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. Author manuscript; available in PMC: 2014 Dec 20.
Published in final edited form as: Science. 2013 Oct 31;342(6165):10.1126/science.1245625. doi: 10.1126/science.1245625

Fig. 1. Overall architecture of a soluble, cleaved, recombinant HIV-1 Env trimer in complex with bnAb PGT 122.

Fig. 1

(A) Schematic of the soluble, cleaved, recombinant HIV-1 Env BG505 SOSIP.664 construct in comparison to full-length gp160. N-linked glycans are shown and numbered on their respective Asn residues. The constant (C1-C5) and variable (V1-V5) regions in gp120 and the fusion peptide (FP), HR1 and HR2 helices, membrane proximal external region (MPER), transmembrane (TM) and cytoplasmic (CT) elements in gp41 are indicated. The SOSIP mutations are shown in red, as well as the added N332 glycan site. The color coding is as in B. (B) Side view of the soluble Env trimer complex with PGT122 showing two of the three Env gp140 protomers associated with PGT122 Fab (blue). A 2Fo-Fc electron density map contoured at 1.0 σ is shown as a gray mesh around the leftmost gp140 protomer. The membrane to which gp41 is attached would be at the bottom of the figure. (C) Side view of the Env trimer. For one of the three protomers on Env, core gp120 is shown in yellow, whereas V1/V2 and V3 regions are highlighted in orange and red, respectively. The main gp41 helical elements are colored in different shades of green. Protein components are rendered according to their secondary structure and glycans are depicted as spheres. (D) View of Env down the trimer axis. Loops of high variability in gp120 (V1-V5) all map to the periphery of the trimer and are labeled. Glycans have been omitted for clarity. Dashed lines indicate the location of gp120 V2 and V4 loops for which electron density was absent or ambiguous. The figure was generated with Pymol (63).