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|Title:||Structural basis for dsRNA recognition by NS1 protein of influenza A virus||Authors:||Cheng, A.
Influenza A virus
Nonstructural protein 1
|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|
|Appears in Collections:||Staff Publications|
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