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Crystal Structure of the Nipah Virus Phosphoprotein Multimerization Domain G519NCrystal Structure of the Nipah Virus Phosphoprotein Multimerization Domain G519N
Structural highlights
Function[PHOSP_NIPAV] Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template (By similarity). May play a role to prevent the establishment of cellular antiviral state by binding to host STAT1 in the cytoplasm. This activity is not as strong as that of V and W. Publication Abstract from PubMedNipah virus is a highly lethal zoonotic pathogen found in Southeast Asia that has caused human encephalitis outbreaks with 40%-70% mortality. NiV encodes its own RNA-dependent RNA polymerase within the large protein, L. Efficient polymerase activity requires the phosphoprotein, P, which tethers L to its template, the viral nucleocapsid. P is a multifunctional protein with modular domains. The central P multimerization domain is composed of a long, tetrameric coiled coil. We investigated the importance of structural features found in this domain for polymerase function using a newly constructed NiV bicistronic minigenome assay. We identified a conserved basic patch and central kink in the coiled coil that are important for polymerase function, with R555 being absolutely essential. This basic patch and central kink are conserved in the related human pathogens measles and mumps viruses, suggesting that this mechanism may be conserved. A Conserved Basic Patch and Central Kink in the Nipah Virus Phosphoprotein Multimerization Domain Are Essential for Polymerase Function.,Bruhn JF, Hotard AL, Spiropoulou CF, Lo MK, Saphire EO Structure. 2019 Feb 13. pii: S0969-2126(19)30012-7. doi:, 10.1016/j.str.2019.01.012. PMID:30799076[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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