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dc.contributor.authorKerry, Philip Stephen
dc.contributor.authorLong, E
dc.contributor.authorTaylor, Margaret Alexandra
dc.contributor.authorRussell, Rupert James Martin
dc.date.accessioned2012-07-17T15:31:01Z
dc.date.available2012-07-17T15:31:01Z
dc.date.issued2011-08-01
dc.identifier.citationKerry , P S , Long , E , Taylor , M A & Russell , R J M 2011 , ' Conservation of a crystallographic interface suggests a role for beta-sheet augmentation in influenza virus NS1 multifunctionality ' , Acta Crystallographica. Section F, Structural biology and crystallization communications , vol. 67 , no. 8 , pp. 858-861 . https://doi.org/10.1107/S1744309111019312en
dc.identifier.issn1744-3091
dc.identifier.otherPURE: 9019845
dc.identifier.otherPURE UUID: d3835aec-8c78-4fb5-b3e5-11ae41e893e4
dc.identifier.otherScopus: 80051509830
dc.identifier.urihttp://hdl.handle.net/10023/2996
dc.descriptionThis research was supported by grants from the Medical Research Council (MRC) and the Scottish Funding Council (SFC).en
dc.description.abstractThe effector domain (ED) of the influenza virus virulence factor NS1 is capable of interaction with a variety of cellular and viral targets, although regulation of these events is poorly understood. Introduction of a W187A mutation into the ED abolishes dimer formation; however, strand-strand interactions between mutant NS1 ED monomers have been observed in two previous crystal forms. A new condition for crystallization of this protein [0.1 M Bis-Tris pH 6.0, 0.2 M NaCl, 22%(w/v) PEG 3350, 20 mM xylitol] was discovered using the hanging-drop vapour-diffusion method. Diffraction data extending to 1.8 Å resolution were collected from a crystal grown in the presence of 40 mM thieno[2,3-b]pyridin-2-ylmethanol. It was observed that there is conservation of the strand-strand interface in crystals of this monomeric NS1 ED in three different space groups. This observation, coupled with conformational changes in the interface region, suggests a potential role for [beta]-sheet augmentation in NS1 function.
dc.language.isoeng
dc.relation.ispartofActa Crystallographica. Section F, Structural biology and crystallization communicationsen
dc.rightsCopyright © Kerry et al. 2011. This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.en
dc.subjectEffector domainsen
dc.subjectInfluenza virusen
dc.subjectVirulence factorsen
dc.subjectNS1en
dc.subjectβ-sheet augmentationen
dc.subjectQR355 Virologyen
dc.subject.lccQR355en
dc.titleConservation of a crystallographic interface suggests a role for beta-sheet augmentation in influenza virus NS1 multifunctionalityen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.1107/S1744309111019312
dc.description.statusPeer revieweden


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