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Comment
. 2010 Aug 11;18(8):894-6.
doi: 10.1016/j.str.2010.07.002.

RIG-I "sees" the 5'-triphosphate

Chao Zheng  1 , Hao Wu
Affiliations
Comment

RIG-I "sees" the 5'-triphosphate

Chao Zheng et al. Structure. .

Abstract

RIG-I protects host cells against various RNA viruses by sensing viral RNAs in the cytoplasm. Crystal structures of RIG-I C-terminal domain bound to 5'-triphosphate dsRNA unveils how RIG-I recognizes the 5'-triphosphate moiety, a hallmark of viral RNAs (Lu et al., 2010).

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Figures

Figure 1
Figure 1. RNA Recognition and Activation of RIG-I
(A) Recognition of 5′-ppp dsRNA by RIG-I CTD. RIG-I CTD (gray) and the first six pairs of the dsRNA (pink) are shown as ribbons. 5′-ppp and critical residues for 5′-ppp interaction are shown as stick models with atoms P in yellow, O in red, C in green, and N in blue. Residue F853 of RIG-I CTD, which stacks over the terminal base pair, is shown in cyan. (B) A model of RNA-induced RIG-I activation. RIG-I may exist in an auto-inhibited conformation in the absence of viral RNAs. Upon RNA-binding, RIG-I may open up to allow oligomerization and recruitment of downstream signaling proteins such as MAVS.
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