title: Visualizing the determinants of viral RNA recognition by innate immune sensor RIG-I.
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.
authors.affiliation: Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA.
authors.forename: Dahai
authors.initials: D
authors.lastname: Luo
authors.forename: Andrew
authors.initials: A
authors.lastname: Kohlway
authors.forename: Adriana
authors.initials: A
authors.lastname: Vela
authors.forename: Anna Marie
authors.initials: AM
authors.lastname: Pyle
mesh_terms: D000071457:DEAD Box Protein 58; D053487:DEAD-box RNA Helicases / Q000276:immunology*; D006801:Humans; D007113:Immunity, Innate; D008958:Models, Molecular; D012367:RNA, Viral / Q000378:metabolism*; D011971:Receptors, Immunologic
chemical_list: D012367:RNA, Viral; D011971:Receptors, Immunologic; C452820:RIGI protein, human; D000071457:DEAD Box Protein 58; D053487:DEAD-box RNA Helicases