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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. (c) 2008 Elsevier Inc. All rights reserved.
Original language | English |
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Pages (from-to) | 1-5 |
Number of pages | 5 |
Journal | Virology |
Volume | 378 |
DOIs | |
Publication status | Published - 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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Dive into the research topics of 'Structure of an avian influenza A NS1 protein effector domain'. Together they form a unique fingerprint.Projects
- 1 Finished
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Virus NS1 - PI3 G0601126: Studies on the interaction of influenza virus NS1 protein with cellular P13-kinase
Randall, R. E. (PI)
1/10/07 → 31/12/10
Project: Standard