Visualizing the determinants of viral RNA recognition by innate immune sensor RIG-I

Structure. 2012 Nov 7;20(11):1983-8. doi: 10.1016/j.str.2012.08.029. Epub 2012 Sep 27.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • DEAD Box Protein 58
  • DEAD-box RNA Helicases / immunology*
  • Humans
  • Immunity, Innate*
  • Models, Molecular
  • RNA, Viral / metabolism*

Substances

  • RNA, Viral
  • DDX58 protein, human
  • DEAD Box Protein 58
  • DEAD-box RNA Helicases