Please use this identifier to cite or link to this item: https://doi.org/10.1038/cr.2008.288
Title: Structural basis for dsRNA recognition by NS1 protein of influenza A virus
Authors: Cheng, A.
Wong, S.M. 
Yuan, Y.A. 
Keywords: Crystal structure
Influenza A virus
Nonstructural protein 1
Protein-RNA complex
Issue Date: Feb-2009
Citation: Cheng, A.,Wong, S.M.,Yuan, Y.A. (2009-02). Structural basis for dsRNA recognition by NS1 protein of influenza A virus. Cell Research 19 (2) : 187-195. ScholarBank@NUS Repository. https://doi.org/10.1038/cr.2008.288
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 1.7. 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 α-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. © 2009 IBCB.
Source Title: Cell Research
URI: http://scholarbank.nus.edu.sg/handle/10635/101743
ISSN: 10010602
DOI: 10.1038/cr.2008.288
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