Crystal structure of an avian influenza polymerase PAN reveals an endonuclease active site-Reference-Cited by-同舟云学术

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Crystal structure of an avian influenza polymerase PAN reveals an endonuclease active site

Published:2009-02-04 Issue:7240 Volume:458 Page:909-913
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Yuan Puwei,Bartlam Mark,Lou Zhiyong,Chen Shoudeng,Zhou Jie,He Xiaojing,Lv Zongyang,Ge Ruowen,Li Xuemei,Deng Tao,Fodor Ervin,Rao Zihe,Liu Yingfang

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature07720.pdf

Reference35 articles.

1. Poch, O., Sauvaget, I., Delarue, M. & Tordo, N. Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. EMBO J. 8, 3867–3874 (1989)

2. Li, M. L., Rao, P. & Krug, R. M. The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits. EMBO J. 20, 2078–2086 (2001)

3. Guilligay, D. et al. The structural basis for cap binding by influenza virus polymerase subunit PB2. Nature Struct. Mol. Biol. 15, 500–506 (2008)

4. Fechter, P. et al. Two aromatic residues in the PB2 subunit of influenza A RNA polymerase are crucial for cap binding. J. Biol. Chem. 278, 20381–20388 (2003)

5. Hara, K., Schmidt, F. I., Crow, M. & Brownlee, G. G. Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding. J. Virol. 80, 7789–7798 (2006)

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