{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Murali A"],"funding":["NIAID NIH HHS"],"pagination":["15825-33"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2414291"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["283(23)"],"pubmed_abstract":["RNA recognition receptors are important for detection of and response to viral infections. RIG-I and MDA5 are cytoplasmic DEX(D/H) helicase proteins that can induce signaling in response to RNA ligands, including those from viral infections. LGP2, a homolog of RIG-I and MDA5 without the caspase recruitment domain required for signaling, plays an important role in modulating signaling by MDA5 and RIG-I, presumably through heterocomplex formation and/or by serving as a sink for RNAs. Here we demonstrate that LGP2 can be coexpressed with RIG-I to inhibit activation of the NF-kappaB reporter expression and that LGP2 protein produced in insect cells can bind both single- and double-stranded RNA (dsRNA), with higher affinity and cooperativity for dsRNA. Electron microscopy and image reconstructi"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Structure and function of LGP2, a DEX(D/H) helicase that regulates the innate immunity response."],"pmcid":["PMC2414291"],"funding_grant_id":["1R01AI073335"],"pubmed_authors":["Murali A","Li X","Kao CC","Ranjith-Kumar CT","Li P","Holzenburg A","Bhardwaj K"],"additional_accession":[]},"is_claimable":false,"name":"Structure and function of LGP2, a DEX(D/H) helicase that regulates the innate immunity response.","description":"RNA recognition receptors are important for detection of and response to viral infections. RIG-I and MDA5 are cytoplasmic DEX(D/H) helicase proteins that can induce signaling in response to RNA ligands, including those from viral infections. LGP2, a homolog of RIG-I and MDA5 without the caspase recruitment domain required for signaling, plays an important role in modulating signaling by MDA5 and RIG-I, presumably through heterocomplex formation and/or by serving as a sink for RNAs. Here we demonstrate that LGP2 can be coexpressed with RIG-I to inhibit activation of the NF-kappaB reporter expression and that LGP2 protein produced in insect cells can bind both single- and double-stranded RNA (dsRNA), with higher affinity and cooperativity for dsRNA. Electron microscopy and image reconstructi","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Jun","modification":"2026-05-01T16:55:22.976Z","creation":"2019-03-27T00:15:24Z"},"accession":"S-EPMC2414291","cross_references":{"pubmed":["18411269"],"doi":["10.1074/jbc.m800542200","10.1074/jbc.M800542200"]}}