The structure of the effector domain of the influenza protein NS1, a validated antiviral drug target, has been solved in two space groups

Monzingo, Arthur F.

Robertus, Jon D.

Xia, Shuangluo

Acta Crystallographica Section D Biological Crystallography

English

PubMed

Shuangluo Xia

Arthur F. Monzingo

Jon D. Robertus

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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.NIH grants AI 074497, 075509Robert A. Welch FoundationCenter for Structural Biology from the College of Natural
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Structure of NS1A effector domain from the influenza A/Udorn/72 virus

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