Journal
NUCLEIC ACIDS RESEARCH
Volume 44, Issue 17, Pages 8407-8416Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkw525
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Funding
- National Research Foundation of Korea (NRF), Korean Government [2011-0020322, 2015R1A2A1A15055329, 2015R1A2A2A01005688, 2012M3A9B4027955, 2011-0020334, 2013R1A2A2A05003837, NRF-2015M3A9C4076320]
- Next Generation BioGreen 21 Program [SSAC] [PJ01117701]
- Korea Health Technology R&D Project through the Korea Health Industry Development Institute [HI14C0211]
- National Research Council of Science and Technology [DRC-14-2-KRISS]
- National Research Foundation of Korea [2011-0020334, 2011-0020322, 2015M3A9C4076320, 2015R1A2A1A15055329, 2015R1A2A2A01005688, 2013R1A2A2A05003837, 2012M3A9B4027955] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Retinoic acid-inducible gene I (RIG-I) recognizes specific molecular patterns of viral RNAs for inducing type I interferon. The C-terminal domain (CTD) of RIG-I binds to double-stranded RNA (dsRNA) with the 5'-triphosphate (5'-PPP), which induces a conformational change in RIG-I to an active form. It has been suggested that RIG-I detects infection of influenza A virus by recognizing the 5'-triphosphorylated panhandle structure of the viral RNA genome. Influenza panhandle RNA has a unique structure with a sharp helical bending. In spite of extensive studies of how viral RNAs activate RIG-I, whether the structural elements of the influenza panhandle RNA confer the ability to activate RIG-I signaling has been poorly explored. Here, we investigated the dynamics of the influenza panhandle RNA in complex with RIG-I CTD using NMR spectroscopy and showed that the bending structure of the panhandle RNA negates the requirement of a 5'-PPP moiety for RIG-I activation.
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