The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus.

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 protein

SUBMITTER: Shen Q 

PROVIDER: S-EPMC6717002 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature