Hale, B.G. , Barclay, W.S., Randall, R.E. and Russell, R.J. (2008) Structure of an avian influenza A virus NS1 protein effector domain. Virology, 378(1), pp. 1-5. (doi: 10.1016/j.virol.2008.05.026)
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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.
Item Type: | Articles |
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Keywords: | Influenza |
Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Hale, Dr Benjamin |
Authors: | Hale, B.G., Barclay, W.S., Randall, R.E., and Russell, R.J. |
Subjects: | Q Science > Q Science (General) Q Science > QH Natural history > QH345 Biochemistry Q Science > QR Microbiology > QR355 Virology |
College/School: | College of Medical Veterinary and Life Sciences > School of Infection & Immunity |
Journal Name: | Virology |
ISSN: | 0042-6822 |
Published Online: | 27 June 2008 |
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