2ZKO

Structural basis for dsRNA recognition by NS1 protein of human influenza virus A

Summary for 2ZKO

• Entry DOI: 10.2210/pdb2zko/pdb
• Descriptor: RNA (5'-R(P*AP*GP*AP*CP*AP*GP*CP*AP*UP*UP*AP*UP*GP*CP*UP*GP*UP*CP*UP*UP*U)-3'), Non-structural protein 1, GLYCEROL, ... (4 entities in total)
• Functional Keywords: dsrna, protein-rna interaction, host-virus interaction, interferon antiviral system evasion, nucleus, rna-binding, suppressor of rna silencing, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Influenza A virus
• Cellular location: Host nucleus: P03496
• Total number of polymer chains: 4
• Total formula weight: 30105.00

Authors

Yuan, Y.A. (deposition date: 2008-03-26, release date: 2008-10-14, Last modification date: 2023-11-01)

Primary citation

Cheng, A.,Wong, S.M.,Yuan, Y.A.
Structural basis for dsRNA recognition by NS1 protein of influenza A virus
Cell Res., 19:187-195, 2009

PubMed Abstract: Influenza A viruses are important human pathogens causing periodic pandemic threats. Nonstructural protein 1 (NS1) protein of influenza A virus (NS1A) shields the virus against host defense. Here, we report the crystal structure of NS1A RNA-binding domain (RBD) bound to a double-stranded RNA (dsRNA) at 1.7A. NS1A RBD forms a homodimer to recognize the major groove of A-form dsRNA in a length-independent mode by its conserved concave surface formed by dimeric anti-parallel alpha-helices. dsRNA is anchored by a pair of invariable arginines (Arg38) from both monomers by extensive hydrogen bonds. In accordance with the structural observation, isothermal titration calorimetry assay shows that the unique Arg38-Arg38 pair and two Arg35-Arg46 pairs are crucial for dsRNA binding, and that Ser42 and Thr49 are also important for dsRNA binding. Agrobacterium co-infiltration assay further supports that the unique Arg38 pair plays important roles in dsRNA binding in vivo.Cell Research (2009) 19:187-195. doi: 10.1038/cr.2008.288; published online 23 September 2008.

PubMed: 18813227
DOI: 10.1038/cr.2008.288

Experimental method

X-RAY DIFFRACTION (1.7 Å)