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题名:Structure of the SARS Coronavirus Nucleocapsid Protein RNA-binding Dimerization Domain Suggests a Mechanism for Helical Packaging of Viral RNA
作者:Chun-Yuan Chen, Chung-ke Chang, Yi-Wei Chang, Shih-Che Sue, Hsin-I Bai, Lilianty Riang, Chwan-Deng Hsiao and Tai-huang Huang
来源:Journal of Molecular Biology[IF=5.229], In Press, Corrected Proof, Available online 5 March 2007,
URL :http://dx.doi.org/10.1016/j.jmb.2007.02.069
日期:070415
摘要: Chun-Yuan Chen1, 2, ?, Chung-ke Chang3, ?, Yi-Wei Chang1, Shih-Che Sue3, Hsin-I Bai3, Lilianty Riang3, Chwan-Deng Hsiao1, , and Tai-huang Huang3, 4, ,

1Institute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan, ROC
2Graduate Institute of Cell and Molecular Biology, Taipei Medical University, Taipei 110, Taiwan, ROC
3Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan, ROC
4Department of Physics, National Taiwan Normal University, Taipei, Taiwan, ROC

Received 14 December 2006; revised 15 February 2007; accepted 17 February 2007. Edited by J. Doudna. Available online 5 March 2007.

Summary

Coronavirus nucleocapsid proteins are basic proteins that encapsulate viral genomic RNA to form part of the virus structure. The nucleocapsid protein of SARS-CoV is highly antigenic and associated with several host-cell interactions. Our previous studies using nuclear magnetic resonance revealed the domain organization of the SARS-CoV nucleocapsid protein. RNA has been shown to bind to the N-terminal domain (NTD), although recently the C-terminal half of the protein has also been implicated in RNA binding. Here, we report that the C-terminal domain (CTD), spanning residues 248C365 (NP248-365), had stronger nucleic acid-binding activity than the NTD. To determine the molecular basis of this activity, we have also solved the crystal structure of the NP248-365 region. Residues 248C280 form a positively charged groove similar to that found in the infectious bronchitis virus (IBV) nucleocapsid protein. Furthermore, the positively charged surface area is larger in the SARS-CoV construct than in the IBV. Interactions between residues 248C280 and the rest of the molecule also stabilize the formation of an octamer in the asymmetric unit. Packing of the octamers in the crystal forms two parallel, basic helical grooves, which may be oligonucleotide attachment sites, and suggests a mechanism for helical RNA packaging in the virus. 26.

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