Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 17, Issue 7, Pages 781-U19Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1863
Keywords
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Funding
- Abby Rockefeller Mauze Trust
- Maloris Foundation
- Austrian Science fund FWF [I317]
- Bundesministerium fur Bildung und Forschung Biofuture and GoBio
- Deutsche Forschungsgemeinschaft [SFB704, SFB670, SFB832, KFO177]
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RIG-I is a cytosolic helicase that senses 5'-ppp RNA contained in negative-strand RNA viruses and triggers innate antiviral immune responses. Calorimetric binding studies established that the RIG-I C-terminal regulatory domain (CTD) binds to blunt-end double-stranded 5'-ppp RNA a factor of 17 more tightly than to its single-stranded counterpart. Here we report on the crystal structure of RIG-I CTD bound to both blunt ends of a self-complementary 5'-ppp dsRNA 12-mer, with interactions involving 5'-pp clearly visible in the complex. The structure, supported by mutation studies, defines how a lysine-rich basic cleft within the RIG-I CTD sequesters the observable 5'-pp of the bound RNA, with a stacked phenylalanine capping the terminal base pair. Key intermolecular interactions observed in the crystalline state are retained in the complex of 5'-ppp dsRNA 24-mer and full-length RIG-I under in vivo conditions, as evaluated from the impact of binding pocket RIG-I mutations and 2'-OCH3 RNA modifications on the interferon response.
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