5bxz | pdb_00005bxz

H17 Bat Influenza NS1 RNA Binding Domain

spinqualitylabelsall models 5bxz, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5bxz is a 2 chain structure with sequence from Influenza A virus (A/little yellow-shouldered bat/Guatemala/153/2009(H17N10)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H6QM79_I09A8 Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor/CPSF4 and the poly(A)-binding protein 2/PABPN1. In turn, unprocessed 3' end pre-mRNAs accumulate in the host nucleus and are no longer exported to the cytoplasm. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism. Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated RIGI ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors IRF3 and IRF7. Also binds poly(A) and U6 snRNA. Inhibits the integrated stress response (ISR) in the infected cell by blocking dsRNA binding by EIF2AK2/PKR and further phosphorylation of EIF2S1/EIF-2ALPHA. Stress granule formation is thus inhibited, which allows protein synthesis and viral replication.[RuleBase:RU362113] Publication Abstract from PubMed We demonstrate that novel bat HL17NL10 and HL18NL11 influenza virus NS1 proteins are effective interferon-antagonists, but do not block general host gene expression. Solving the RNA-binding domain structures revealed the canonical NS1 symmetrical homodimer, and RNA-binding required conserved basic residues in this domain. Interferon-antagonism was strictly dependent on RNA-binding, and chimeric bat influenza viruses expressing NS1s defective in this activity were highly attenuated in interferon-competent cells, but not in cells unable to establish antiviral immunity. Novel Bat Influenza Virus NS1 Proteins Bind Double-Stranded RNA and Antagonize Host Innate Immunity.,Turkington HL, Juozapaitis M, Kerry PS, Aydillo T, Ayllon J, Garcia-Sastre A, Schwemmle M, Hale BG J Virol. 2015 Aug 5. pii: JVI.01430-15. PMID:26246567 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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