Nucleocapsid Protein CTD domain, Virus (His)

Nucleocapsid Protein CTD domain, Virus (His) is the C-terminal dimerisation domain (CTD) of nucleocapsid protein in coronaviruses. Nucleocapsid Protein CTD domain has a stronger nucleic acid-binding activity than the NTD, which could be a nucleic acid-binding site^[1] [2].

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].

Virus

E. coli

N-6*His

QHD43423.2

43740575  [NCBI]

N/A

Approximately 16.0 kDa

Greater than 90% as determined by reducing SDS-PAGE.

Solution.

Supplied as a 0.2 μm filter solution of PBS, 2 M Urea, pH 7.4.

<1 EU/μg, determined by LAL method.

Stored at -80°C for 1 year. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.

• [1]. Sander van Boheemen, et al. Genomic characterization of a newly discovered coronavirus associated with acute respiratory distress syndrome in humans. mBio. 2012 Nov 20;3(6):e00473-12.  [Content Brief]

  [2]. Chun-Yuan Chen, et al. Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA. J Mol Biol. 2007 May 11;368(4):1075-86.  [Content Brief]