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

ABSTRACT: 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.

SUBMITTER: Xia S

PROVIDER: S-EPMC2628972 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature

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

Xia Shuangluo S Monzingo Arthur F AF Robertus Jon D JD

Acta crystallographica. Section D, Biological crystallography 20081218 Pt 1

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 confo ...[more]

PMID: 19153461

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