The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Structural Insights into RNA Recognition by RIG-I
Open accessAbstract
Summary Intracellular RIG-I-like receptors (RLRs, including RIG-I, MDA-5, and LGP-2) recognize viral RNAs as pathogen-associated molecular patterns (PAMPs) and initiate an antiviral immune response. To understand the molecular basis of this process, we determined the crystal structure of RIG-I in complex with double-stranded RNA. The dsRNA is sheathed within a network of protein domains that include a conserved “helicase” domain (regions HEL1 and HEL2), a specialized insertion domain (HEL2i), and a C-terminal regulatory domain (CTD). A V-shaped pincer connects HEL2 and the CTD by gripping an α-helical shaft that extends from HEL1. In this way, the pincer coordinates functions of all the domains and couples RNA binding with ATP hydrolysis. RIG-I falls within the Dicer-RIG-I clade of super family 2 of helicases and this structure reveals complex interplay between motor domains, accessory mechanical domains and RNA that has implications for understanding the nanomechanical function this protein family and other ATPases more broadly.
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Metadata
- Authors
- Luo, D., Ding, S. C., Vela, A., Kohlway, A., Lindenbach, B. D., & Pyle, A. M.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2011-10
- Volume
- 147
- Issue
- 2
- Pages
- 409-422
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2158217876
- Cited by
- 419
- References
- 7
- FWCI
- 15.46
- Type
- journal article
- Language
- en
- Open access
- bronze
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