tetano
Editor, Senior Moderator
Biomol NMR Assign
. 2020 Dec 3.
doi: 10.1007/s12104-020-09995-y. Online ahead of print.
[SUP]1[/SUP] H, [SUP]13[/SUP] C, and [SUP]15[/SUP] N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein
Sophie M Korn[SUP] 1 2 [/SUP], Roderick Lambertz[SUP] 1 [/SUP], Boris F?rtig[SUP] 3 2 [/SUP], Martin Hengesbach[SUP] 3 [/SUP], Frank L?hr[SUP] 4 2 [/SUP], Christian Richter[SUP] 3 2 [/SUP], Harald Schwalbe[SUP] 3 2 [/SUP], Julia E Weigand[SUP] 5 [/SUP], Jens W?hnert[SUP] 1 2 [/SUP], Andreas Schlundt[SUP] 6 7 [/SUP]
Affiliations
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.
Keywords: Covid19-NMR; Dimerization domain; Nucleocapsid; Protein druggability; SARS-CoV-2; Solution NMR-spectroscopy; Structural protein.
. 2020 Dec 3.
doi: 10.1007/s12104-020-09995-y. Online ahead of print.
[SUP]1[/SUP] H, [SUP]13[/SUP] C, and [SUP]15[/SUP] N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein
Sophie M Korn[SUP] 1 2 [/SUP], Roderick Lambertz[SUP] 1 [/SUP], Boris F?rtig[SUP] 3 2 [/SUP], Martin Hengesbach[SUP] 3 [/SUP], Frank L?hr[SUP] 4 2 [/SUP], Christian Richter[SUP] 3 2 [/SUP], Harald Schwalbe[SUP] 3 2 [/SUP], Julia E Weigand[SUP] 5 [/SUP], Jens W?hnert[SUP] 1 2 [/SUP], Andreas Schlundt[SUP] 6 7 [/SUP]
Affiliations
- PMID: 33270159
- DOI: 10.1007/s12104-020-09995-y
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.
Keywords: Covid19-NMR; Dimerization domain; Nucleocapsid; Protein druggability; SARS-CoV-2; Solution NMR-spectroscopy; Structural protein.