ArticleBiochemical and biophysical research communications2019
The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus.
Article in Biochemical and biophysical research communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Nonstructural Protein 1 of Influenza A (NS1A) Demonstrates Strain-Specific dsRNA Binding Capabilities.ACS infectious diseases · 2025Article
- Influenza A Virus NS1 Protein Structural Flexibility Analysis According to Its Structural Polymorphism Using Computational Approaches.International journal of molecular sciences · 2022Article
- Article
- Molecular recognition of a host protein by NS1 of pandemic and seasonal influenza A viruses.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Central Role of Non-Structural Protein 1 (NS1) in Influenza Biology and Infection.International journal of molecular sciences · 2020Review
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Authors and funding
2 authors at 1 institution in 1 country.
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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.
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