2N74

Solution Structure of the RNA-Binding domain of non-structural protein 1 from the 1918 H1N1 influenza virus

Summary for 2N74

• Entry DOI: 10.2210/pdb2n74/pdb
• NMR Information: BMRB: 25793
• Descriptor: Non-structural protein 1 (1 entity in total)
• Functional Keywords: ns1, rig-i, virulence, viral protein
• Biological source: Influenza A virus
• Cellular location: Host nucleus: Q99AU3
• Total number of polymer chains: 2
• Total formula weight: 16818.99

Authors

Jureka, A.S.,Kleinpeter, A.B.,Cornilescu, G.,Cornilescu, C.C.,Schwieters, C.D.,Petit, C.M. (deposition date: 2015-09-03, release date: 2015-09-30, Last modification date: 2024-05-15)

Primary citation

Jureka, A.S.,Kleinpeter, A.B.,Cornilescu, G.,Cornilescu, C.C.,Petit, C.M.
Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I.
Structure, 23:2001-2010, 2015

PubMed 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.

PubMed: 26365801
DOI: 10.1016/j.str.2015.08.007

Experimental method

SOLUTION NMR