Extended Data Fig. 3: Comparison of IFIT structures, related to Fig. 2. | Nature Microbiology

Extended Data Fig. 3: Comparison of IFIT structures, related to Fig. 2.

From: The IFIT2–IFIT3 antiviral complex targets short 5’ untranslated regions on viral mRNAs for translation inhibition

Extended Data Fig. 3

(a) Model of the IFIT2-IFIT3 heterodimer, colored by Q score, which measures the agreement of each residue with the experimental map. (b) IFIT2-IFIT3 model colored by protomer with IFIT2 blue and IFIT3 yellow, and experimental cryoEM map contoured around the IFIT2 protomer (top left), contoured around the IFIT3 protomer (bottom right), or showing the full map (bottom right). (c) Linear representation of human IFIT1 and mouse IFIT2 and IFIT3 domains showing helix numbers and subdomains (SDs). (d) Structure of capped RNA-bound IFIT1 (PDB 6C6K ref. 26), colored by SD as in panel c. (e) (Left) Structure of mouse IFIT2 extracted from the IFIT2-IFIT3 heterodimer, colored by SD as in panel c. The green helices represent the domain-swapped helices during IFIT2-IFIT3 heterodimer formation. (Right) Mouse IFIT2 overlaid with IFIT1 (gray) bound to capped RNA (black). (f) Same as panel e, but with mouse IFIT3.

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