Unknown

Dataset Information

0

The structural basis of 5' triphosphate double-stranded RNA recognition by RIG-I C-terminal domain.

ABSTRACT: RIG-I is a cytosolic sensor of viral RNA that plays crucial roles in the induction of type I interferons. The C-terminal domain (CTD) of RIG-I is responsible for the recognition of viral RNA with 5' triphosphate (ppp). However, the mechanism of viral RNA recognition by RIG-I is still not fully understood. Here, we show that RIG-I CTD binds 5' ppp dsRNA or ssRNA, as well as blunt-ended dsRNA, and exhibits the highest affinity for 5' ppp dsRNA. Crystal structures of RIG-I CTD bound to 5' ppp dsRNA with GC- and AU-rich sequences revealed that RIG-I recognizes the termini of the dsRNA and interacts with the 5' ppp through extensive electrostatic interactions. Mutagenesis and RNA-binding studies demonstrated that similar binding surfaces are involved in the recognition of different forms of RNA. Mutations of key residues at the RNA-binding surface affected RIG-I signaling in cells.

SUBMITTER: Lu C 

PROVIDER: S-EPMC2919622 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

The structural basis of 5' triphosphate double-stranded RNA recognition by RIG-I C-terminal domain.

Lu Cheng C   Xu Hengyu H   Ranjith-Kumar C T CT   Brooks Monica T MT   Hou Tim Y TY   Hu Fuqu F   Herr Andrew B AB   Strong Roland K RK   Kao C Cheng CC   Li Pingwei P  

Structure (London, England : 1993) 20100715 8

RIG-I is a cytosolic sensor of viral RNA that plays crucial roles in the induction of type I interferons. The C-terminal domain (CTD) of RIG-I is responsible for the recognition of viral RNA with 5' triphosphate (ppp). However, the mechanism of viral RNA recognition by RIG-I is still not fully understood. Here, we show that RIG-I CTD binds 5' ppp dsRNA or ssRNA, as well as blunt-ended dsRNA, and exhibits the highest affinity for 5' ppp dsRNA. Crystal structures of RIG-I CTD bound to 5' ppp dsRNA  ...[more]

Similar Datasets

Unknown Structural basis of siRNA recognition by TRBP double-stranded RNA binding domains.
| S-EPMC5852647 | biostudies-literature
Unknown Crystal structure of RIG-I C-terminal domain bound to blunt-ended double-strand RNA without 5' triphosphate.
| S-EPMC3045611 | biostudies-literature
Unknown Cytosolic viral sensor RIG-I is a 5'-triphosphate-dependent translocase on double-stranded RNA.
| S-EPMC3567915 | biostudies-literature
Unknown Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III.
| S-EPMC420390 | biostudies-literature
Unknown Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus.
| S-EPMC2824854 | biostudies-literature
Unknown RNA recognition by a Staufen double-stranded RNA-binding domain.
| S-EPMC305639 | biostudies-literature
Unknown Molecular basis for transfer RNA recognition by the double-stranded RNA-binding domain of human dihydrouridine synthase 2.
| S-EPMC6451096 | biostudies-literature
Unknown The regulatory domain of the RIG-I family ATPase LGP2 senses double-stranded RNA.
| S-EPMC2665237 | biostudies-literature
Unknown Structural basis for single-stranded RNA recognition and cleavage by C3PO.
| S-EPMC5100593 | biostudies-literature
Unknown Structural basis of chimpanzee APOBEC3H dimerization stabilized by double-stranded RNA.
| S-EPMC6212771 | biostudies-literature