Summary information and primary citation

PDB-id
4ay2; DSSR-derived features in text and JSON formats
Class
hydrolase-RNA
Method
X-ray (2.8 Å)
Summary
Capturing 5' tri-phosphorylated RNA duplex by rig-i
Reference
Luo D, Kohlway A, Vela A, Pyle AM (2012): "Visualizing the Determinants of Viral RNA Recognition by Innate Immune Sensor Rig-I." Structure, 20, 1983. doi: 10.1016/J.STR.2012.08.029.
Abstract
Retinoic acid inducible gene-I (RIG-I) is a key intracellular immune receptor for pathogenic RNAs, particularly from RNA viruses. Here, we report the crystal structure of human RIG-I bound to a 5' triphosphorylated RNA hairpin and ADP nucleotide at 2.8 Å resolution. The RNA ligand contains all structural features that are essential for optimal recognition by RIG-I, as it mimics the panhandle-like signatures within the genome of negative-stranded RNA viruses. RIG-I adopts an intermediate, semiclosed conformation in this product state of ATP hydrolysis. The structure of this complex allows us to visualize the first steps in RIG-I recognition and activation upon viral infection.

Cartoon-block schematics in six views (download the tarball)

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