Structure of NS1A effector domain from the influenza A/Udorn/72 virus

被引:38
作者
Xia, Shuangluo [1 ]
Monzingo, Arthur F. [1 ]
Robertus, Jon D. [1 ]
机构
[1] Univ Texas Austin, Dept Chem & Biochem, Inst Cellular & Mol Biol, Austin, TX 78712 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2009年 / 65卷
关键词
A VIRUS; RNA-BINDING; PROTEIN; CELLS;
D O I
10.1107/S0907444908032186
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:11 / 17
页数:7
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