The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Structural and functional insights into 5′-ppp RNA pattern recognition by the innate immune receptor RIG-I
Open accessAbstract
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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Metadata
- Authors
- Wang, Y., Ludwig, J., Schuberth, C., Goldeck, M., Schlee, M., Li, H., Juranek, S., Sheng, G., Micura, R., Tuschl, T., Hartmann, G., & Patel, D. J.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2010-06-27
- Volume
- 17
- Issue
- 7
- Pages
- 781-787
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2039294169
- Cited by
- 254
- References
- 36
- FWCI
- 8.66
- Type
- journal article
- Language
- en
- Open access
- green
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