Structure of an avian influenza A virus NS1 protein effector domain.
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.
Hale
Benjamin G
BG
Centre for Biomolecular Sciences, University of St. Andrews, St. Andrews, Fife, KY16 9ST, UK.
Barclay
Wendy S
WS
Randall
Richard E
RE
Russell
Rupert J
RJ
D000818:Animals; D002942:Circular Dichroism; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D004372:Ducks / Q000821:virology*; D006801:Humans; D009980:Influenza A virus / Q000378:metabolism*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017361:Viral Nonstructural Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
C085820:INS1 protein, influenza virus; D017361:Viral Nonstructural Proteins