5dil | pdb_00005dil
Crystal structure of the effector domain of the NS1 protein from influenza virus B
Structural highlights
FunctionX2C382_9INFB Binds and inhibits the ubiquitin-like protein G1P2/ISG15, which is an early antiviral protein. Inhibits IRF-3 nuclear translocation and activation. Inhibits IFN-beta promoter activation; this inhibition is not dsRNA-binding dependent Prevents EIF2AK2/PKR activation, either by binding double strand RNA or by interacting directly with EIF2AK2/PKR. Also binds poly(A) and U6 snRNA. Suppresses the RNA silencing-based antiviral response in Drosophila cells.[PIRNR:PIRNR003938] Publication Abstract from PubMedInfluenza viruses cause a highly contagious respiratory disease in humans. The NS1 proteins of influenza A and B viruses (NS1A and NS1B proteins, respectively) are composed of two domains, a dimeric N-terminal domain and a C-terminal domain, connected by a flexible polypeptide linker. Here we report the 2.0-A X-ray crystal structure and nuclear magnetic resonance studies of the NS1B C-terminal domain, which reveal a novel and unexpected basic RNA-binding site that is not present in the NS1A protein. We demonstrate that single-site alanine replacements of basic residues in this site lead to reduced RNA-binding activity, and that recombinant influenza B viruses expressing these mutant NS1B proteins are severely attenuated in replication. This novel RNA-binding site of NS1B is required for optimal influenza B virus replication. Most importantly, this study reveals an unexpected RNA-binding function in the C-terminal domain of NS1B, a novel function that distinguishes influenza B viruses from influenza A viruses. A Second RNA-Binding Site in the NS1 Protein of Influenza B Virus.,Ma LC, Guan R, Hamilton K, Aramini JM, Mao L, Wang S, Krug RM, Montelione GT Structure. 2016 Sep 6;24(9):1562-72. doi: 10.1016/j.str.2016.07.001. Epub 2016, Aug 18. PMID:27545620[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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