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Publication Abstract from PubMed

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 A 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.

Visualizing the Determinants of Viral RNA Recognition by Innate Immune Sensor RIG-I.,Luo D, Kohlway A, Vela A, Pyle AM Structure. 2012 Nov 7;20(11):1983-8. doi: 10.1016/j.str.2012.08.029. Epub 2012, Sep 27. PMID:23022350^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.