4o6i
2.0A crystal structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-terminal Domain
Structural highlights
FunctionNCAP_LYCVA Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as template for viral transcription and replication. The increased presence of protein N in host cell does not seem to trigger the switch from transcription to replication as observed in other negative strain RNA viruses. Disables the host innate defense by interfering with beta interferon (IFNB) production through the inhibition of host IRF3 phosphorylation and activation by host IKBKE. Through the interaction with host IKBKE, strongly inhibits the phosphorylation and nuclear translocation of IRF3, a protein involved in IFN activation pathway, leading to the inhibition of IFNB and IRF3-dependent promoters activation.[1] [2] [3] Publication Abstract from PubMedThe X-ray crystal structure of the Lymphocytic choriomeningitis virus nucleoprotein C-terminal immunosuppressive domain (LCMV NPDelta340) was determined to 2.0 A resolution. The structure indicates that LCMV NPDelta340, like the other structurally characterized arenaviral nucleoproteins, adopts the fold of an exonuclease. This structure provides a crucial three-dimensional template for functional exploration of the replication and immunosuppression of this prototypic arenavirus. Structure of the LCMV nucleoprotein provides a template for understanding arenavirus replication and immunosuppression.,West BR, Hastie KM, Saphire EO Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1764-9. doi:, 10.1107/S1399004714007883. Epub 2014 May 30. PMID:24914986[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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