Please use this identifier to cite or link to this item: https://doi.org/10.1038/nature07120
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dc.titleCrystal structure of the polymerase PAC-PB1N complex from an avian influenza H5N1 virus
dc.contributor.authorHe, X.
dc.contributor.authorZhou, J.
dc.contributor.authorBartlam, M.
dc.contributor.authorZhang, R.
dc.contributor.authorMa, J.
dc.contributor.authorLou, Z.
dc.contributor.authorLi, X.
dc.contributor.authorLi, J.
dc.contributor.authorJoachimiak, A.
dc.contributor.authorZeng, Z.
dc.contributor.authorGe, R.
dc.contributor.authorRao, Z.
dc.contributor.authorLiu, Y.
dc.date.accessioned2014-10-27T08:25:04Z
dc.date.available2014-10-27T08:25:04Z
dc.date.issued2008-08-28
dc.identifier.citationHe, X., Zhou, J., Bartlam, M., Zhang, R., Ma, J., Lou, Z., Li, X., Li, J., Joachimiak, A., Zeng, Z., Ge, R., Rao, Z., Liu, Y. (2008-08-28). Crystal structure of the polymerase PAC-PB1N complex from an avian influenza H5N1 virus. Nature 454 (7208) : 1123-1126. ScholarBank@NUS Repository. https://doi.org/10.1038/nature07120
dc.identifier.issn00280836
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100370
dc.description.abstractThe recent emergence of highly pathogenic avian influenza A virus strains with subtype H5N1 pose a global threat to human health. Elucidation of the underlying mechanisms of viral replication is critical for development of anti-influenza virus drugs. The influenza RNA-dependent RNA polymerase (RdRp) heterotrimer has crucial roles in viral RNA replication and transcription. It contains three proteins: PA, PB1 and PB2. PB1 harbours polymerase and endonuclease activities and PB2 is responsible for cap binding; PA is implicated in RNA replication and proteolytic activity, although its function is less clearly defined. Here we report the 2.9 ångström structure of avian H5N1 influenza A virus PA (PAC, residues 257-716) in complex with the PA-binding region of PB1 (PB1N, residues 1-25). PAC has a fold resembling a dragon's head with PB1N clamped into its open 'jaws'. PB1N is a known inhibitor that blocks assembly of the polymerase heterotrimer and abolishes viral replication. Our structure provides details for the binding of PB1N to PAC at the atomic level, demonstrating a potential target for novel anti-influenza therapeutics. We also discuss a potential nucleotide binding site and the roles of some known residues involved in polymerase activity. Furthermore, to explore the role of PA in viral replication and transcription, we propose a model for the influenza RdRp heterotrimer by comparing PAC with the λ3 reovirus polymerase structure, and docking the PAC structure into an available low resolution electron microscopy map. ©2008 Macmillan Publishers Limited. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1038/nature07120
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1038/nature07120
dc.description.sourcetitleNature
dc.description.volume454
dc.description.issue7208
dc.description.page1123-1126
dc.description.codenNATUA
dc.identifier.isiut000258719600039
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