Figure 2.
Location of variants on human IFNAR1. (A) Schematic representation of full-length IFNAR1 protein, including the four fibronectin type III subdomains (SD1–4), the signal peptide (SP), and the transmembrane domain (TM). The mutations investigated in this study are depicted on the diagram. The hitherto unknown mutations are indicated in red, and the previously reported mutations are indicated in black. (B) Ribbon representation of the overall structure of the IFNα2–YNS–IFNAR1–IFNAR2 ternary complex (PDB 3SE3 [Thomas et al., 2011], visualized with PyMOL [version 2.5.5]) showing IFNAR1 with SD1 colored in green, SD2 in blue, and SD3 in violet. IFNα2–YNS is depicted in cyan and IFNAR2 in beige. The amino-acid variants of IFNAR1 described here are highlighted by the depiction of their side chains as spheres across IFNAR1 SD1-3. Variants resulting from a missense mutation are depicted with side chains in yellow. Variants resulting in a complete LOF for IFN-α2, IFN-ω, and IFN-β signaling or hypomorphic for such signaling are depicted with side chains in magenta. In-frame indel variants are depicted with side chains in orange. Variants resulting from a frameshift mutation or an early stop codon (F45fs, W114X, T208fs, V225fs, and W261X) are not shown. (C) Close-up view of IFNAR1 SD1 (green) showing the location of variants N44 (orange), W73, and C79 (both magenta), along with V96 and the adjacent M128 from IFNAR1 SD2 (yellow). The locations of SD1 in relation to IFNAR1 SD2 (blue) and IFNα2-YNS (cyan) are shown. (D) Close-up view of IFNAR1 SD2 (blue), showing the location of P103, M128, and Y215 variants and the adjacent V96 from IFNAR1 SD1 (yellow), together with I144 (magenta). The locations of IFNAR1 SD2 (slate blue) in relation to IFNAR1 SD1 (green), IFNAR1 SD3 (violet), and IFNα2-YNS (cyan) are shown. (E) Close-up view of IFNAR1 SD3 (violet) showing the locations of the variants A264 (yellow) and S316 (magenta). The approximate locations of P334 (yellow circle) and P335 (orange circle), which were not resolved in the IFNα2–YNS–IFNAR1–IFNAR2 crystal structure, are predicted. The locations of IFNAR1 SD3 (violet) in relation to IFNAR1 SD2 (blue) and IFNα2-YNS (cyan) are shown.

Location of variants on human IFNAR1. (A) Schematic representation of full-length IFNAR1 protein, including the four fibronectin type III subdomains (SD1–4), the signal peptide (SP), and the transmembrane domain (TM). The mutations investigated in this study are depicted on the diagram. The hitherto unknown mutations are indicated in red, and the previously reported mutations are indicated in black. (B) Ribbon representation of the overall structure of the IFNα2–YNS–IFNAR1–IFNAR2 ternary complex (PDB 3SE3 [Thomas et al., 2011], visualized with PyMOL [version 2.5.5]) showing IFNAR1 with SD1 colored in green, SD2 in blue, and SD3 in violet. IFNα2–YNS is depicted in cyan and IFNAR2 in beige. The amino-acid variants of IFNAR1 described here are highlighted by the depiction of their side chains as spheres across IFNAR1 SD1-3. Variants resulting from a missense mutation are depicted with side chains in yellow. Variants resulting in a complete LOF for IFN-α2, IFN-ω, and IFN-β signaling or hypomorphic for such signaling are depicted with side chains in magenta. In-frame indel variants are depicted with side chains in orange. Variants resulting from a frameshift mutation or an early stop codon (F45fs, W114X, T208fs, V225fs, and W261X) are not shown. (C) Close-up view of IFNAR1 SD1 (green) showing the location of variants N44 (orange), W73, and C79 (both magenta), along with V96 and the adjacent M128 from IFNAR1 SD2 (yellow). The locations of SD1 in relation to IFNAR1 SD2 (blue) and IFNα2-YNS (cyan) are shown. (D) Close-up view of IFNAR1 SD2 (blue), showing the location of P103, M128, and Y215 variants and the adjacent V96 from IFNAR1 SD1 (yellow), together with I144 (magenta). The locations of IFNAR1 SD2 (slate blue) in relation to IFNAR1 SD1 (green), IFNAR1 SD3 (violet), and IFNα2-YNS (cyan) are shown. (E) Close-up view of IFNAR1 SD3 (violet) showing the locations of the variants A264 (yellow) and S316 (magenta). The approximate locations of P334 (yellow circle) and P335 (orange circle), which were not resolved in the IFNα2–YNS–IFNAR1–IFNAR2 crystal structure, are predicted. The locations of IFNAR1 SD3 (violet) in relation to IFNAR1 SD2 (blue) and IFNα2-YNS (cyan) are shown.

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