Fig. 2 | Nature Communications

Fig. 2

From: Rationally designed carbohydrate-occluded epitopes elicit HIV-1 Env-specific antibodies

Fig. 2

Structural characterization of designed CONE immunogens. a Crystal structure of C2S5 (PDB 6CFE) aligned to the design model (left) and to the gp120 CONE 2 region (middle, PDB 5FYL, clade A sequence), with the epitope shown as sticks; (Right) Close-up view of the alignment between grafted resides in C2S5 (slate) and the gp120 (yellow) residues in their native conformations. b Crystal structure of C4S3 (PDB 6CBU) with the CONE 4 epitope shown as sticks (slate). c Secondary structure assignment based on solution NMR mapped to the C1S1 design model (left). Plot of the differences of chemical shifts ΔCα−ΔCβ (middle) for each residue of C1S1 indicates which residues adopt α-helical (>1 ppm, dark cyan) or β-sheet (<−1 ppm, yellow) structures. (Right) 1H-15N HSQC spectrum with the assignments to CONE 1 residues indicated. Source data are provided as a Source Data file. See also Supplementary Fig. 9

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