<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Murali A</submitter><funding>NIAID NIH HHS</funding><pagination>15825-33</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2414291</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>283(23)</volume><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</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>Structure and function of LGP2, a DEX(D/H) helicase that regulates the innate immunity response.</pubmed_title><pmcid>PMC2414291</pmcid><funding_grant_id>1R01AI073335</funding_grant_id><pubmed_authors>Murali A</pubmed_authors><pubmed_authors>Li X</pubmed_authors><pubmed_authors>Kao CC</pubmed_authors><pubmed_authors>Ranjith-Kumar CT</pubmed_authors><pubmed_authors>Li P</pubmed_authors><pubmed_authors>Holzenburg A</pubmed_authors><pubmed_authors>Bhardwaj K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structure and function of LGP2, a DEX(D/H) helicase that regulates the innate immunity response.</name><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</description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Jun</publication><modification>2026-05-01T16:55:22.976Z</modification><creation>2019-03-27T00:15:24Z</creation></dates><accession>S-EPMC2414291</accession><cross_references><pubmed>18411269</pubmed><doi>10.1074/jbc.m800542200</doi><doi>10.1074/jbc.M800542200</doi></cross_references></HashMap>