5dil | pdb_00005dil

Crystal structure of the effector domain of the NS1 protein from influenza virus B

spinqualitylabelsall models 5dil, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dil is a 2 chain structure with sequence from Influenza b virus (b/singapore/dso_090134/2004). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: IOD NonStd Res: MSE Gene: NS1 (Influenza B virus (B/Singapore/DSO_090134/2004)) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [X2C382_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 PubMed Influenza 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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