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Structure of an avian influenza A virus NS1 protein effector domain
- Source :
- Virology. (1):1-5
- Publisher :
- Elsevier Inc.
-
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.
- Subjects :
- Circular dichroism
Protein Conformation
Viral protein
viruses
NS1
Avian influenza
Viral Nonstructural Proteins
Biology
Crystallography, X-Ray
medicine.disease_cause
Protein Structure, Secondary
Virulence factor
Avian Influenza A Virus
Protein structure
Virology
Influenza A virus
medicine
Animals
Humans
X-ray crystallography
Effector
Circular Dichroism
virus diseases
biochemical phenomena, metabolism, and nutrition
Influenza A virus subtype H5N1
Cell biology
Ducks
Interferon-antagonist
Crystallization
Dimerization
Subjects
Details
- Language :
- English
- ISSN :
- 00426822
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Virology
- Accession number :
- edsair.doi.dedup.....75abc29b15a1645f462812da70320b23
- Full Text :
- https://doi.org/10.1016/j.virol.2008.05.026