Nucleocapsid Protein CTD domain, Virus (His)

Coronaviruses are enveloped viruses with a positive-sense RNA genomeand and has a nucleocapsid of helical symmetry. The Nucleocapsid Protein localize to the cytoplasm and the nucleolus in both virus-infected primary cells and in cells transfected with plasmids that express N protein. Nucleocapsid Protein is a basic protein and is abundant in coronaviruses, which has nonspecific binding activity toward nucleic acids, including ssRNA, ssDNA, and dsDNA^[1].
SARS-CoV N protein contains two distinct RNA-binding domains (the N-terminal domain [NTD] and the CTD, they are linked by a poorly structured linkage region. The CTD spanning residues 248 to 365 shows stronger nucleic acid-binding activity than the NTD and the basic region between residues 248 to 280 of CTD forms a positively charged groove that represents a likely binding region for RNA. Additionally, crystal structures of CoV NPs-CTDs provide structural clues on how the building blocks for coronavirus nucleocapsid form through NP dimer^[2].