Structural highlights
Publication Abstract from PubMed
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.
Structure of an avian influenza A virus NS1 protein effector domain.,Hale BG, Barclay WS, Randall RE, Russell RJ Virology. 2008 Aug 15;378(1):1-5. Epub 2008 Jun 27. PMID:18585749[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hale BG, Barclay WS, Randall RE, Russell RJ. Structure of an avian influenza A virus NS1 protein effector domain. Virology. 2008 Aug 15;378(1):1-5. Epub 2008 Jun 27. PMID:18585749 doi:http://dx.doi.org/S0042-6822(08)00364-4