tetano
Editor, Senior Moderator
Biochem Biophys Res Commun. 2019 Aug 14. pii: S0006-291X(19)31538-4. doi: 10.1016/j.bbrc.2019.08.027. [Epub ahead of print]
[h=1]The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus.[/h] Shen Q[SUP]1[/SUP], Cho JH[SUP]2[/SUP].
[h=3]Author information[/h] 1 Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA. 2 Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA. Electronic address: jaehyuncho@tamu.edu.
[h=3]Abstract[/h] Nonstructural protein 1 (NS1) is a multifunctional virulence factor of influenza virus. The effector domain (ED) of influenza viruses is capable of binding to a variety of host factors, however, the molecular basis of the interactions remains to be investigated. The isolated NS1-ED exists in equilibrium between the monomer and homodimer. Although the structural diversity of the dimer interface has been well-characterized, limited information is available regarding the internal conformational heterogeneity of the monomeric NS1-ED. Here, we present the solution NMR structure of the NS1-ED W187R of the 1918 influenza A virus, which caused the "Spanish flu." Structural plasticity is an essential property to understand the molecular mechanism by which NS1-ED interacts with multiple host proteins. Structural comparison with the NS1-ED from influenza A/Udorn/1972 (Ud) strain revealed a similar overall structure but a distinct conformational variation and flexibility. Our results suggest that conformational flexibility of the NS1-ED might differ depending on the influenza strain.
Copyright ? 2019 Elsevier Inc. All rights reserved.
[h=4]KEYWORDS:[/h] 1918 influenza A virus; Conformational dynamics; NMR; Nonstructural protein 1; Structural plasticity; Virulence factor
PMID: 31420169 DOI: 10.1016/j.bbrc.2019.08.027
[h=1]The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus.[/h] Shen Q[SUP]1[/SUP], Cho JH[SUP]2[/SUP].
[h=3]Author information[/h] 1 Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA. 2 Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA. Electronic address: jaehyuncho@tamu.edu.
[h=3]Abstract[/h] Nonstructural protein 1 (NS1) is a multifunctional virulence factor of influenza virus. The effector domain (ED) of influenza viruses is capable of binding to a variety of host factors, however, the molecular basis of the interactions remains to be investigated. The isolated NS1-ED exists in equilibrium between the monomer and homodimer. Although the structural diversity of the dimer interface has been well-characterized, limited information is available regarding the internal conformational heterogeneity of the monomeric NS1-ED. Here, we present the solution NMR structure of the NS1-ED W187R of the 1918 influenza A virus, which caused the "Spanish flu." Structural plasticity is an essential property to understand the molecular mechanism by which NS1-ED interacts with multiple host proteins. Structural comparison with the NS1-ED from influenza A/Udorn/1972 (Ud) strain revealed a similar overall structure but a distinct conformational variation and flexibility. Our results suggest that conformational flexibility of the NS1-ED might differ depending on the influenza strain.
Copyright ? 2019 Elsevier Inc. All rights reserved.
[h=4]KEYWORDS:[/h] 1918 influenza A virus; Conformational dynamics; NMR; Nonstructural protein 1; Structural plasticity; Virulence factor
PMID: 31420169 DOI: 10.1016/j.bbrc.2019.08.027