PDBsum entry 2n74

Viral protein

PDB id: 2n74

Contents

Protein chains

73 a.a.

PDB id:

2n74

Name:

Viral protein

Title:

Solution structure of the RNA-binding domain of non-structural protein 1 from the 1918 h1n1 influenza virus

Structure:

Non-structural protein 1. Chain: a, b. Fragment: RNA binding domain (unp residues 1-73). Synonym: ns1, ns1a. Engineered: yes

Source:

Influenza a virus. Organism_taxid: 88776. Strain: a/brevig mission/1/1918 h1n1. Gene: ns. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

16 models

Authors:

A.S.Jureka,A.B.Kleinpeter,G.Cornilescu,C.C.Cornilescu,C.D.Schwieters, C.M.Petit

Key ref:

A.S.Jureka et al. (2015). Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I. Structure, 23, 2001-2010. PubMed id: 26365801 DOI: 10.1016/j.str.2015.08.007

Date:

03-Sep-15 Release date: 30-Sep-15

Protein chains

Q99AU3  (NS1_I18A0) -  Non-structural protein 1 from Influenza A virus (strain A/Brevig Mission/1/1918 H1N1)

Seq: 230 a.a.

Struc: 73 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.str.2015.08.007

Structure 23:2001-2010 (2015)

PubMed id: 26365801

Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I.

A.S.Jureka, A.B.Kleinpeter, G.Cornilescu, C.C.Cornilescu, C.M.Petit.

ABSTRACT

The influenza non-structural protein 1 (NS1) plays a critical role in antagonizing the innate immune response to infection. One interaction that facilitates this function is between NS1 and RIG-I, one of the main sensors of influenza virus infection. While NS1 and RIG-I are known to interact, it is currently unclear whether this interaction is direct or if it is mediated by other biomolecules. Here we demonstrate a direct, strain-dependent interaction between the NS1 RNA binding domain (NS1(RBD)) of the influenza A/Brevig Mission/1918 H1N1 (1918(H1N1)) virus and the second caspase activation and recruitment domain of RIG-I. Solving the solution structure of the 1918(H1N1) NS1(RBD) revealed features in a functionally novel region that may facilitate the observed interaction. The biophysical and structural data herein suggest a possible mechanism by which strain-specific differences in NS1 modulate influenza virulence.