3RVC

Effector domain of NS1 from influenza A/PR/8/34 containing a W187A mutation

Summary for 3RVC

• Entry DOI: 10.2210/pdb3rvc/pdb
• Related: 3O9Q 3O9R
• Descriptor: Non-structural protein 1 (2 entities in total)
• Functional Keywords: interferon antagonist, protein binding
• Biological source: Influenza A virus
• Cellular location: Host nucleus: P03496
• Total number of polymer chains: 1
• Total formula weight: 16875.51

Authors

Kerry, P.S.,Long, E.,Taylor, M.A.,Russell, R.J.M. (deposition date: 2011-05-06, release date: 2011-08-24, Last modification date: 2024-02-28)

Primary citation

Kerry, P.S.,Long, E.,Taylor, M.A.,Russell, R.J.
Conservation of a crystallographic interface suggests a role for beta-sheet augmentation in influenza virus NS1 multifunctionality.
Acta Crystallogr.,Sect.F, 67:858-861, 2011

PubMed 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.

PubMed: 21821881
DOI: 10.1107/S1744309111019312

Experimental method

X-RAY DIFFRACTION (1.8 Å)