title: Conservation of a crystallographic interface suggests a role for β-sheet augmentation in influenza virus NS1 multifunctionality.
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 β-sheet augmentation in NS1 function.
authors.affiliation: Biomedical Sciences Research Complex, University of St Andrews, St Andrews, Fife, Scotland. psk5@st-andrews.ac.uk
authors.forename: Philip S
authors.initials: PS
authors.lastname: Kerry
authors.forename: Elizabeth
authors.initials: E
authors.lastname: Long
authors.forename: Margaret A
authors.initials: MA
authors.lastname: Taylor
authors.forename: Rupert J M
authors.initials: RJ
authors.lastname: Russell
mesh_terms: D018360:Crystallography, X-Ray; D008958:Models, Molecular; D009975:Orthomyxoviridae / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017361:Viral Nonstructural Proteins / Q000737:chemistry*
chemical_list: C085820:INS1 protein, influenza virus; D017361:Viral Nonstructural Proteins