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. Author manuscript; available in PMC: 2016 May 19.
Published in final edited form as: Immunity. 2015 May 19;42(5):815–825. doi: 10.1016/j.immuni.2015.04.015

Figure 2. mIL-2:JES6-1 and mIL-2:S4B6 complex structures reveal basis for competitive binding between anti-IL-2 antibodies and IL-2 receptor.

Figure 2

(A) Orthosteric views of the hIL-2 cytokine-receptor quaternary complex (PDB ID 2B5I) comprised of hIL-2 (pink), IL-2Rα (cyan), IL-2Rβ (navy), and IL-2Rγ (gold). (B) Overlay of the mIL-2:JES6-1 and mIL-2:S4B6 complex structures on the hIL-2 quaternary complex. Both JES6-1-bound mIL-2 (dark gray) and S4B6-bound mIL-2 (light gray) are presented, with the JES6-1 variable heavy (VH, blue) and light (VL, magenta) and the S4B6 VH (orange) and VL (green) chains shown as surface representations. Crystallographic statistics for mIL-2:antibody complexes are provided in Table S1. (C) “Top-down” (left) and “bottom-up” (right) views of JES6-1-bound mIL-2 (dark gray) and S4B6-bound mIL-2 (light gray) with the predicted binding epitopes of IL-2Ra (cyan), IL-2Rβ (navy), IL-2R (gold), JES6-1 (blue), and S4B6 (orange) on the mIL-2 cytokine shaded. Residues shared between the mIL-2:antibody and the mIL-2:IL-2Ra, mIL-2:IL-2Rβ, or mIL-2:IL-2R interfaces are colored red. Venn diagrams at bottom indicate the relative extent of overlap between the antibody and receptor epitopes. Also see Figure S2.