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. Author manuscript; available in PMC: 2019 Jul 1.
Published in final edited form as: Nat Med. 2018 Jun 25;24(7):1005–1014. doi: 10.1038/s41591-018-0070-2

Fig. 4 |. The IL-2-F5111 complex structure reveals that the F5111 Fab obstructs the IL-2Rβ-binding site on IL-2.

Fig. 4 |

a, The IL-2-F5111 complex superimposed on the IL-2-receptor quaternary complex (PDB code 2B5I) shows steric obstruction of IL-2Rβ by the Fab. The F5111 heavy chain (HC; green) and light chain (LC; cyan) and IL-2 (orange) are shown in surface representation. CD25 (yellow), IL-2Rβ (blue) and γc (magenta) are shown as ribbons. b, IL-2 (surface representation) complexed with F5111 (ribbons) is shown, highlighting the binding sites on IL-2 for the IL-2 receptor complex. c, A ‘top-down’ view comparison of the IL-2 conformations in the IL-2-F5111 complex (orange) and the IL-2-receptor quaternary complex (PDB code 2B5I, olive-yellow) shows that the position of the IL-2 A-B loop in the IL-2-F5111 complex is incompatible with CD25 binding. IL-2 is shown as a ribbon while CD25 is shown in surface representation. d, High-resolution depiction of c. The IL-2 residues in the IL-2-F5111 complex that would conflict with CD25 are highlighted in red. The arrows illustrate movements of the A-B and B-C loops induced by F5111 binding. VH, heavy-chain variable domain; VL, light-chain variable domain.