作者: Chung-ke Chang , Ming-Hon Hou , Chi-Fon Chang , Chwan-Deng Hsiao , Tai-huang Huang
DOI: 10.1016/J.ANTIVIRAL.2013.12.009
关键词:
摘要: The nucleocapsid phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV N protein) packages viral genome into a helical ribonucleocapsid (RNP) and plays fundamental role during self-assembly. It is protein with multifarious activities. In this article we will review our current understanding structure its interaction nucleic acid. Highlights progresses include uncovering modular organization, determining structures structural domains, realizing roles disorder in protein-protein protein-nucleic acid interactions, visualizing ribonucleoprotein inside virions. was also demonstrated that N-protein binds to at multiple sites coupled-allostery manner. We propose SARS-CoV RNP model conforms existing data bears resemblance RNA viruses. highlights critical organization intrinsic formation functions dynamic capsid This paper forms part symposium Antiviral Research on "From SARS MERS: 10 years research highly pathogenic human coronaviruses."