Structure of an avian influenza A NS1 protein effector domain

BG Hale, WS Barclay, Richard Edward Randall, Rupert James Martin Russell

Research output: Contribution to journalArticlepeer-review

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. (c) 2008 Elsevier Inc. All rights reserved.

Original languageEnglish
Pages (from-to)1-5
Number of pages5
JournalVirology
Volume378
DOIs
Publication statusPublished - 15 Aug 2008

Keywords

  • avian influenza
  • NS1
  • X-ray crystallography
  • dimerization
  • interferon-antagonist
  • DOUBLE-STRANDED-RNA
  • BINDING
  • INTERFERON
  • SOFTWARE
  • SEQUENCE
  • PATHWAY

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