6vhi
Crystal structure of the human ILRUN Fw domain
Structural highlights
FunctionILRUN_HUMAN Negative regulator of innate antiviral response. Blocks IRF3-dependent cytokine production such as IFNA, IFNB and TNF (PubMed:29802199). Interacts with IRF3 and inhibits IRF3 recruitment to type I IFN promoter sequences while also reducing nuclear levels of the coactivators EP300 and CREBBP (PubMed:29802199).[1] Publication Abstract from PubMedRegulation of type-I interferon (IFN) production is essential to the balance between antimicrobial defence and autoimmune disorders. The human protein-coding gene ILRUN (inflammation and lipid regulator with UBA-like and NBR1-like domains, previously C6orf106) was recently characterised as an inhibitor of antiviral and proinflammatory cytokine (interferon-alpha/beta and tumor necrosis factor alpha) transcription. Currently there is a paucity of information about the molecular characteristics of ILRUN, despite it being associated with several diseases including virus infection, coronary artery disease, obesity and cancer. Here, we characterise ILRUN as a highly phylogenetically conserved protein containing UBA-like and a NBR1-like domains that are both essential for inhibition of type-I interferon and tumor necrosis factor alpha) transcription in human cells. We also solved the crystal structure of the NBR1-like domain, providing insights into its potential role in ILRUN function. This study provides critical information for future investigations into the role of ILRUN in health and disease. Molecular characterisation of ILRUN, a novel inhibitor of proinflammatory and antimicrobial cytokines.,Ambrose RL, Brice AM, Caputo AT, Alexander MR, Tribolet L, Liu YC, Adams TE, Bean AGD, Stewart CR Heliyon. 2020 Jun 3;6(6):e04115. doi: 10.1016/j.heliyon.2020.e04115. eCollection , 2020 Jun. PMID:32518853[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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