| Literature DB >> 19153461 |
Shuangluo Xia1, Arthur F Monzingo, Jon D Robertus.
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.Entities:
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Year: 2008 PMID: 19153461 PMCID: PMC2628972 DOI: 10.1107/S0907444908032186
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449