6NU0

Solution NMR structure of 1918 NS1 effector domain

Summary for 6NU0

• Entry DOI: 10.2210/pdb6nu0/pdb
• NMR Information: BMRB: 12032
• Descriptor: Non-structural protein 1 (1 entity in total)
• Functional Keywords: virulence factor, hijack host proteins, viral protein
• Biological source: Influenza A virus
• Total number of polymer chains: 1
• Total formula weight: 26073.02

Authors

Shen, Q.,Cho, J.H. (deposition date: 2019-01-30, release date: 2020-01-08, Last modification date: 2024-05-15)

Primary citation

Shen, Q.,Cho, J.H.
The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus.
Biochem.Biophys.Res.Commun., 518:178-182, 2019

PubMed Abstract: 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.

PubMed: 31420169
DOI: 10.1016/j.bbrc.2019.08.027

Experimental method

SOLUTION NMR