Influenza A virus NS1 protein is a multifunctional virulence factor. Here, we report a crystal structure for the NS1 effector domain of avian influenza virus A/Duck/Albany/76. Comparison of this structure with that reported for a human strain shows both proteins share a common monomer conformation, albeit with subtle differences. Strikingly, our data reveal a novel helix-helix dimeric interface between monomers of the avian NS1 protein, which is also found in the human NS1 crystal lattice. We re-evaluate the current model of NS1 dimeric assembly, and provide biochemical evidence to show tryptophan-187 (a residue located at the helix-helix interface) is essential for dimerization of this effector domain. © 2008 Elsevier Inc. All rights reserved.
Hale, B. G., Barclay, W. S., Randall, R. E., & Russell, R. J. (2008). Structure of an avian influenza A virus NS1 protein effector domain. Virology, 378(1), 1–5. https://doi.org/10.1016/j.virol.2008.05.026