Conservation of a crystallographic interface suggests a role for beta-sheet augmentation in influenza virus NS1 multifunctionality

Philip Stephen Kerry, E Long, Margaret Alexandra Taylor, Rupert James Martin Russell

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Abstract

The 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.
Original languageEnglish
Pages (from-to)858-861
JournalActa Crystallographica. Section F, Structural biology and crystallization communications
Volume67
Issue number8
Early online date13 Jul 2011
DOIs
Publication statusPublished - 1 Aug 2011

Keywords

  • Effector domains
  • Influenza virus
  • Virulence factors
  • NS1
  • β-sheet augmentation

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