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Mol Cell. 2008 Feb 29;29(4):428-40. doi: 10.1016/j.molcel.2007.11.028. Epub 2008 Jan 31.

Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses.

Author information

1
Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Hokkaido 060-0812, Japan.

Abstract

A DExD/H protein, RIG-I, is critical in innate antiviral responses by sensing viral RNA. Here we show that RIG-I recognizes two distinct viral RNA patterns: double-stranded (ds) and 5'ppp single-stranded (ss) RNA. The binding of RIG-I with dsRNA or 5'ppp ssRNA in the presence of ATP produces a common structure, as suggested by protease digestion. Further analyses demonstrated that the C-terminal domain of RIG-I (CTD) recognizes these RNA patterns and CTD coincides with the autorepression domain. Structural analysis of CTD by NMR spectroscopy in conjunction with mutagenesis revealed that the basic surface of CTD with a characteristic cleft interacts with RIG-I ligands. Our results suggest that the bipartite structure of CTD regulates RIG-I on encountering viral RNA patterns.

PMID:
18242112
DOI:
10.1016/j.molcel.2007.11.028
[Indexed for MEDLINE]
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