| Literature DB >> 18585749 |
Benjamin G Hale1, Wendy S Barclay, Richard E Randall, Rupert J Russell.
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.Entities:
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Year: 2008 PMID: 18585749 DOI: 10.1016/j.virol.2008.05.026
Source DB: PubMed Journal: Virology ISSN: 0042-6822 Impact factor: 3.616