Abstract
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.
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