- 作者: 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
- 作者服務機構: 1 Institute of Biomedical Sciences, Academia S璯ica, Nankang, Taipei, Taiwan, ROC; ; 2 Department of Physics, National Taiwan Normal University, Taipei, Taiwan, ROC; ; 3 Department of Agronomy, National Taiwan University, Taipei, Taiwan, ROC; ; 4 Institute of Biological Chemistry, Academia S璯ica, Nankang, Taipei, Taiwan, ROC
- 中文摘要: --
- 英文摘要: 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. Bioin-formatics 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.
- 中文關鍵字: --
- 英文關鍵字: capsid protein, coronavirus, domain arrangement, intrinsically disordered protein, NMR, oligomerization, SARS