Open AccessCrystallization and preliminary crystallographic studies of human RIG‐I in complex with double‐stranded RNA
Author(s) -
Moon Hyunjin,
Choe Jungwoo
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109018405
Subject(s) - rig i , rna , rna helicase a , rna silencing , crystallization , biology , gene , escherichia coli , microbiology and biotechnology , repressor , gene expression , crystallography , chemistry , helicase , biochemistry , rna interference , organic chemistry
Retinoic acid inducible gene‐I (RIG‐I) is an essential component of the innate immune system that is responsible for the detection and elimination of invading viruses. RIG‐I recognizes viral RNAs inside the cell and then initiates downstream signalling to activate the IRF‐3 and NF‐κB genes, which results in the production of type I interferons. RIG‐I is composed of an N‐terminal CARD domain for signalling and C‐terminal helicase and repressor domains for RNA recognition. A RIG‐I–RNA binding assay was performed to investigate the in vitro RIG‐I–RNA binding properties. Selenomethionine‐incorporated RIG‐I was expressed using Escherichia coli and purified for crystallization. X‐ray data were collected from RIG‐I–dsRNA complex crystals to 2.8 Å resolution using synchrotron radiation.