RIG-I

2LWD, 2LWE, 2QFB, 2QFD, 2RMJ, 2YKG, 3LRN, 3LRR, 3NCU, 3OG8, 3ZD6, 3ZD7, 4AY2, 4BPB, 4NQK, 4ON9, 4P4H, 5E3H, 5F98, 5F9F, 5F9H23586230073ENSG00000107201ENSMUSG00000040296O95786Q6Q899NM_014314NM_172689NP_055129NP_766277RIG-I (retinoic acid-inducible gene I) is a RIG-I-like receptor dsRNA helicase enzyme that is encoded (in humans) by the DDX58 gene. RIG-I is part of the RIG-I-like receptor family, which also includes MDA5 and LGP2, and functions as a pattern recognition receptor that is a sensor for viruses such as influenza A, Sendai virus, and flavivirus. Certain retroviruses, such as HIV-1, encode a protease that directs RIG-I to the lysosome for degradation, and thereby evade RIG-I mediated signaling. RIG-I typically recognizes short (< 4000 nt) 5′ triphosphate uncapped double stranded or single stranded RNA. RIG-I and MDA5 are involved in activating MAVS and triggering an antiviral response. RIG-I is also able to detect non-self 5′-triphosphorylated dsRNA transcribed from AT-rich dsDNA by DNA-dependent RNA polymerase III (Pol III). For many viruses, effective RIG-I-mediated antiviral responses are dependent on functionally active LGP2. RIG-I (retinoic acid-inducible gene I) is a RIG-I-like receptor dsRNA helicase enzyme that is encoded (in humans) by the DDX58 gene. RIG-I is part of the RIG-I-like receptor family, which also includes MDA5 and LGP2, and functions as a pattern recognition receptor that is a sensor for viruses such as influenza A, Sendai virus, and flavivirus. Certain retroviruses, such as HIV-1, encode a protease that directs RIG-I to the lysosome for degradation, and thereby evade RIG-I mediated signaling. RIG-I typically recognizes short (< 4000 nt) 5′ triphosphate uncapped double stranded or single stranded RNA. RIG-I and MDA5 are involved in activating MAVS and triggering an antiviral response. RIG-I is also able to detect non-self 5′-triphosphorylated dsRNA transcribed from AT-rich dsDNA by DNA-dependent RNA polymerase III (Pol III). For many viruses, effective RIG-I-mediated antiviral responses are dependent on functionally active LGP2. DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases which are implicated in a number of cellular processes involving RNA binding and alteration of RNA secondary structure. RIG-I contains a RNA helicase-DEAD box motifs and a caspase recruitment domain (CARD). RIG-I is involved in viral double-stranded (ds) RNA recognition and the regulation of immune response.