Structure of the SARS Coronavirus Nucleocapsid Protein RNA-binding Dimerization Domain Suggests a Mechanism for Helical Packaging of Viral RNA

Chun Yuan Chen, Chung ke Chang, Yi Wei Chang, Shih Che Sue, Hsin I. Bai, Lilianty Riang, Chwan Deng Hsiao*, Tai huang Huang

*此作品的通信作者

研究成果: 雜誌貢獻期刊論文同行評審

192 引文 斯高帕斯(Scopus)

摘要

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 248-365 (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 248-280 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 248-280 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.

原文英語
頁(從 - 到)1075-1086
頁數12
期刊Journal of Molecular Biology
368
發行號4
DOIs
出版狀態已發佈 - 2007 5月 11

ASJC Scopus subject areas

  • 生物物理學
  • 結構生物學
  • 分子生物學

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