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Curr Opin Struct Biol. 2014 Apr;25:25-33. doi: 10.1016/j.sbi.2013.11.011. Epub 2013 Dec 20.

Parts, assembly and operation of the RIG-I family of motors.

Author information

1
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, United States.
2
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, United States; Department of Chemistry, Yale University, New Haven, CT 06520, United States; Howard Hughes Medical Institute, Chevy Chase, MD 20815, United States. Electronic address: anna.pyle@yale.edu.

Abstract

Host cell invasion is monitored by a series of pattern recognition receptors (PRRs) that activate the innate immune machinery upon detection of a cognate pathogen associated molecular pattern (PAMP). The RIG-I like receptor (RLR) family of PRRs includes three proteins--RIG-I, MDA5, and LGP2--responsible for the detection of intracellular pathogenic RNA. All RLR proteins are built around an ATPase core homologous to those found in canonical Superfamily 2 (SF2) RNA helicases, which has been modified through the addition of novel accessory domains to recognize duplex RNA. This review focuses on the structural bases for pathogen-specific dsRNA binding and ATPase activation in RLRs, differential RNA recognition by RLR family members, and implications for other duplex RNA activated ATPases, such as Dicer.

PMID:
24878341
PMCID:
PMC4070197
DOI:
10.1016/j.sbi.2013.11.011
[Indexed for MEDLINE]
Free PMC Article

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