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. Author manuscript; available in PMC: 2019 Dec 12.
Published in final edited form as: Immunity. 2018 Mar 20;48(3):474–476. doi: 10.1016/j.immuni.2018.03.001

Figure 1. The IFIT1-IFIT3 Complex Preferentially Binds to Cap 0 RNA.

Figure 1.

On the left side of the panel, IFIT1 alone can bind to both cap 0 (guanine N7-methylated) and 5′-ppp RNA molecules, but the cap 0 binding has a higher affinity. On the right side is the complex of IFIT1 with the C-terminal domain (CTD) of IFIT3. This complex binds to cap 0 RNA with higher affinity than IFIT1 alone does and loses detectable binding to 5′-ppp RNA. The complex formation further increases IFIT1 stability.