Structure of NS1A effector domain from the influenza A/Udorn/72 virus.
The nonstructural protein NS1A from influenza virus is a multifunctional virulence factor and a potent inhibitor of host immunity. It has two functional domains: an N-terminal 73-amino-acid RNA-binding domain and a C-terminal effector domain. Here, the crystallographic structure of the NS1A effector domain of influenza A/Udorn/72 virus is presented. Structure comparison with the NS1 effector domain from mouse-adapted influenza A/Puerto Rico/8/34 (PR8) virus strain reveals a similar monomer conformation but a different dimer interface. Further analysis and evaluation shows that the dimer interface observed in the structure of the PR8 NS1 effector domain is likely to be a crystallographic packing effect. A hypothetical model of the intact NS1 dimer is presented.
Xia
Shuangluo
S
Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, University of Texas, 1 University Station A5300, Austin, TX 78712, USA.
Monzingo
Arthur F
AF
Robertus
Jon D
JD
D024322:Amino Acids, Aromatic / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D006801:Humans; D009980:Influenza A virus / Q000737:chemistry* / Q000378:metabolism; D051379:Mice; D008958:Models, Molecular; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D012367:RNA, Viral / Q000378:metabolism; D040681:Structural Homology, Protein; D017361:Viral Nonstructural Proteins / Q000737:chemistry* / Q000378:metabolism
D024322:Amino Acids, Aromatic; C085820:INS1 protein, influenza virus; D012367:RNA, Viral; D017361:Viral Nonstructural Proteins