3LRN

Crystal structure of human RIG-I CTD bound to a 14 bp GC 5' ppp dsRNA

Summary for 3LRN

• Entry DOI: 10.2210/pdb3lrn/pdb
• Descriptor: Probable ATP-dependent RNA helicase DDX58, RNA (5'-R(*(GTP)P*GP*CP*GP*CP*GP*CP*GP*CP*GP*CP*GP*CP*C)-3'), ZINC ION, ... (4 entities in total)
• Functional Keywords: innate immunity, viral rna sensing, rig-i like receptors, antiviral defense, atp-binding, helicase, immune response, metal-binding, nucleotide-binding, rna-binding, hydrolase-rna complex, hydrolase/rna
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: O95786
• Total number of polymer chains: 4
• Total formula weight: 37873.28

Authors

Li, P. (deposition date: 2010-02-11, release date: 2010-06-02, Last modification date: 2024-04-03)

Primary citation

Lu, C.,Xu, H.,Ranjith-Kumar, C.T.,Brooks, M.T.,Hou, T.Y.,Hu, F.,Herr, A.B.,Strong, R.K.,Kao, C.C.,Li, P.
The Structural Basis of 5' Triphosphate Double-Stranded RNA Recognition by RIG-I C-Terminal Domain.
Structure, 18:1032-1043, 2010

PubMed 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.

PubMed: 20637642
DOI: 10.1016/j.str.2010.05.007

Experimental method

X-RAY DIFFRACTION (2.6 Å)