Interferon-induced protein with tetratricopeptide repeats 5

Definition:

Interferon-induced RNA-binding protein involved in the human innate immune response. Has a broad and adaptable RNA structure recognition important for RNA recognition specificity in antiviral defense. Binds precursor and processed tRNAs as well as poly-U-tailed tRNA fragments. Specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and selectively binds AT-rich dsDNA. Additionally, as a mediator in innate immunity, regulates positively IKK-NFKB signaling by sinergizing the recruitment of IKK to MAP3K7.

References:

[1]. Feng Feng, et al. Crystal structure and nucleotide selectivity of human IFIT5/ISG58. Cell Res. 2013 Aug;23(8):1055-8. [Content Brief]

[2]. Yazan M Abbas, et al. Structural basis for viral 5'-PPP-RNA recognition by human IFIT proteins. Nature. 2013 Feb 7;494(7435):60-4. [Content Brief]

[3]. George E Katibah, et al. tRNA binding, structure, and localization of the human interferon-induced protein IFIT5. Mol Cell. 2013 Feb 21;49(4):743-50. [Content Brief]

[4]. Caishang Zheng, et al. IFIT5 positively regulates NF-κB signaling through synergizing the recruitment of IκB kinase (IKK) to TGF-β-activated kinase 1 (TAK1). Cell Signal. 2015 Dec;27(12):2343-54. [Content Brief]

[5]. George E Katibah, et al. Broad and adaptable RNA structure recognition by the human interferon-induced tetratricopeptide repeat protein IFIT5. Proc Natl Acad Sci U S A. 2014 Aug 19;111(33):12025-30. [Content Brief]

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