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The structure analysis and antigenicity study of the N protein of SARS-CoV / 基因组蛋白质组与生物信息学报·英文版
Genomics, Proteomics & Bioinformatics ; (4): 145-154, 2003.
Article in English | WPRIM | ID: wpr-339513
ABSTRACT
The Coronaviridae family is characterized by a nucleocapsid that is composed of the genome RNA molecule in combination with the nucleoprotein (N protein) within a virion. The most striking physiochemical feature of the N protein of SARS-CoV is that it is a typical basic protein with a high predicted pI and high hydrophilicity, which is consistent with its function of binding to the ribophosphate backbone of the RNA molecule. The predicted high extent of phosphorylation of the N protein on multiple candidate phosphorylation sites demonstrates that it would be related to important functions, such as RNA-binding and localization to the nucleolus of host cells. Subsequent study shows that there is an SR-rich region in the N protein and this region might be involved in the protein-protein interaction. The abundant antigenic sites predicted in the N protein, as well as experimental evidence with synthesized polypeptides, indicate that the N protein is one of the major antigens of the SARS-CoV. Compared with other viral structural proteins, the low variation rate of the N protein with regards to its size suggests its importance to the survival of the virus.
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Full text: Available Index: WPRIM (Western Pacific) Main subject: Phosphorylation / Base Composition / Genetic Variation / Enzyme-Linked Immunosorbent Assay / Molecular Sequence Data / Base Sequence / Cluster Analysis / Amino Acid Sequence / Sequence Analysis, DNA / DNA Primers Language: English Journal: Genomics, Proteomics & Bioinformatics Year: 2003 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Phosphorylation / Base Composition / Genetic Variation / Enzyme-Linked Immunosorbent Assay / Molecular Sequence Data / Base Sequence / Cluster Analysis / Amino Acid Sequence / Sequence Analysis, DNA / DNA Primers Language: English Journal: Genomics, Proteomics & Bioinformatics Year: 2003 Type: Article