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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

234 Citations (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.

Original languageEnglish
Pages (from-to)59-72
Number of pages14
JournalJournal of Biomedical Science
Issue number1
Publication statusPublished - 2006 Jan


  • Capsid protein
  • Coronavirus
  • Domain arrangement
  • Intrinsically disordered protein
  • NMR
  • Oligomerization
  • SARS

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology
  • Biochemistry, medical
  • Pharmacology (medical)


Dive into the research topics of 'Modular organization of SARS coronavirus nucleocapsid protein'. Together they form a unique fingerprint.

Cite this