Modular organization of SARS coronavirus nucleocapsid protein

Chung Ke Chang, Shih Che Sue, Tsan Hung Yu, Chiu Min Hsieh, Cheng Kun Tsai, Yen Chieh Chiang, Shin Jye Lee, Hsin Hao Hsiao, Wen Jin Wu, Wei Lun Chang, Chun Hung Lin, Tai Huang Huang*


研究成果: 雜誌貢獻期刊論文同行評審

231 引文 斯高帕斯(Scopus)


The SARS-CoV nucleocapsid (N) protein is a major antigen in severe acute respiratory syndrome. It binds to the viral RNA genome and forms the ribonucleoprotein core. The SARS-CoV N protein has also been suggested to be involved in other important functions in the viral life cycle. Here we show that the N protein consists of two non-interacting structural domains, the N-terminal RNA-binding domain (RBD) (residues 45-181) and the C-terminal dimerization domain (residues 248-365) (DD), surrounded by flexible linkers. The C-terminal domain exists exclusively as a dimer in solution. The flexible linkers are intrinsically disordered and represent potential interaction sites with other protein and protein-RNA partners. Bioinformatics reveal that other coronavirus N proteins could share the same modular organization. This study provides information on the domain structure partition of SARS-CoV N protein and insights into the differing roles of structured and disordered regions in coronavirus nucleocapsid proteins.

頁(從 - 到)59-72
期刊Journal of Biomedical Science
出版狀態已發佈 - 2006 1月

ASJC Scopus subject areas

  • 內分泌學、糖尿病和代謝
  • 分子生物學
  • 臨床生物化學
  • 細胞生物學
  • 生物化學(醫學)
  • 藥學(醫學)


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