PropertyValue
?:abstract
  • The current outbreak of the highly infectious COVID-19 respiratory disease is caused by the novel coronavirus SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2). To fight the pandemic, the search for promising viral drug targets has become a cross-border common goal of the international biomedical research community. Within the international Covid19-NMR consortium, scientists support drug development against SARS-CoV-2 by providing publicly available NMR data on viral proteins and RNAs. The coronavirus nucleocapsid protein (N protein) is an RNA-binding protein involved in viral transcription and replication. Its primary function is the packaging of the viral RNA genome. The highly conserved architecture of the coronavirus N protein consists of an N-terminal RNA-binding domain (NTD), followed by an intrinsically disordered Serine/Arginine (SR)-rich linker and a C-terminal dimerization domain (CTD). Besides its involvement in oligomerization, the CTD of the N protein (N-CTD) is also able to bind to nucleic acids by itself, independent of the NTD. Here, we report the near-complete NMR backbone chemical shift assignments of the SARS-CoV-2 N-CTD to provide the basis for downstream applications, in particular site-resolved drug binding studies.
is ?:annotates of
?:creator
?:doi
  • 10.1007/s12104-020-09995-y
?:doi
?:journal
  • Biomol_NMR_Assign
?:license
  • cc-by
?:pdf_json_files
  • document_parses/pdf_json/f707f3f6ba62da92709fdad1434b64659bfd5321.json
?:pmc_json_files
  • document_parses/pmc_json/PMC7711055.xml.json
?:pmcid
?:pmid
?:pmid
  • 33270159.0
?:publication_isRelatedTo_Disease
?:sha_id
?:source
  • Medline; PMC
?:title
  • (1)H, (13)C, and (15)N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein
?:type
?:year
  • 2020-12-03

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