Crystal structure of RIG-I C-terminal domain bound to blunt-ended double-strand RNA without 5' triphosphate.

abstract

• RIG-I recognizes molecular patterns in viral RNA to regulate the induction of type I interferons. The C-terminal domain (CTD) of RIG-I exhibits high affinity for 5' triphosphate (ppp) dsRNA as well as blunt-ended dsRNA. Structures of RIG-I CTD bound to 5'-ppp dsRNA showed that RIG-I recognizes the termini of dsRNA and interacts with the ppp through electrostatic interactions. However, the structural basis for the recognition of non-phosphorylated dsRNA by RIG-I is not fully understood. Here, we show that RIG-I CTD binds blunt-ended dsRNA in a different orientation compared to 5' ppp dsRNA and interacts with both strands of the dsRNA. Overlapping sets of residues are involved in the recognition of blunt-ended dsRNA and 5' ppp dsRNA. Mutations at the RNA-binding surface affect RNA binding and signaling by RIG-I. These results provide the mechanistic basis for how RIG-I recognizes different RNA ligands.

authors

• Li, Pingwei

published proceedings

• Nucleic Acids Res

altmetric score

• 3

author list (cited authors)

• Lu, C., Ranjith-Kumar, C. T., Hao, L., Kao, C. C., & Li, P.

citation count

• 54

complete list of authors

• Lu, Cheng||Ranjith-Kumar, CT||Hao, Lujiang||Kao, C Cheng||Li, Pingwei

publication date

• March 2011

publisher

• Oxford University Press (OUP)  Publisher

published in

• Nucleic Acids Research (NAR)  Journal

keywords

• Binding Sites
• Crystallography
• DEAD-box RNA Helicases
• Dead Box Protein 58
• HEK293 Cells
• Humans
• Models, Molecular
• Mutation
• Phosphates
• Protein Binding
• Protein Structure, Tertiary
• RNA, Double-Stranded
• RNA-Binding Proteins
• Signal Transduction

PubMed Central ID

• 20961956

Digital Object Identifier (DOI)

• 10.1093/nar/gkq974

start page

• 1565

end page

• 1575

volume

• 39

issue

• 4

URL

• http%3A%2F%2Fdx.doi.org%2F10.1093%2Fnar%2Fgkq974