tetano
Editor, Senior Moderator
Biomol NMR Assign
. 2020 Aug 8.
doi: 10.1007/s12104-020-09971-6. Online ahead of print.
[SUP]1[/SUP] H, [SUP]13[/SUP] C, and [SUP]15[/SUP] N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e
Sophie M Korn[SUP] 1 2 [/SUP], Karthikeyan Dhamotharan[SUP] 1 2 [/SUP], Boris F?rtig[SUP] 3 2 [/SUP], Martin Hengesbach[SUP] 3 2 [/SUP], Frank L?hr[SUP] 4 2 [/SUP], Nusrat S Qureshi[SUP] 3 2 [/SUP], Christian Richter[SUP] 3 2 [/SUP], Krishna Saxena[SUP] 3 2 [/SUP], Harald Schwalbe[SUP] 3 2 [/SUP], Jan-Niklas Tants[SUP] 1 2 [/SUP], Julia E Weigand[SUP] 5 [/SUP], Jens W?hnert[SUP] 1 2 [/SUP], Andreas Schlundt[SUP] 6 7 [/SUP]
Affiliations
Abstract
The ongoing pandemic caused by the Betacoronavirus SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus-2) demonstrates the urgent need of coordinated and rapid research towards inhibitors of the COVID-19 lung disease. The covid19-nmr consortium seeks to support drug development by providing publicly accessible NMR data on the viral RNA elements and proteins. The SARS-CoV-2 genome encodes for approximately 30 proteins, among them are the 16 so-called non-structural proteins (Nsps) of the replication/transcription complex. The 217-kDa large Nsp3 spans one polypeptide chain, but comprises multiple independent, yet functionally related domains including the viral papain-like protease. The Nsp3e sub-moiety contains a putative nucleic acid-binding domain (NAB) with so far unknown function and consensus target sequences, which are conceived to be both viral and host RNAs and DNAs, as well as protein-protein interactions. Its NMR-suitable size renders it an attractive object to study, both for understanding the SARS-CoV-2 architecture and drugability besides the classical virus' proteases. We here report the near-complete NMR backbone chemical shifts of the putative Nsp3e NAB that reveal the secondary structure and compactness of the domain, and provide a basis for NMR-based investigations towards understanding and interfering with RNA- and small-molecule-binding by Nsp3e.
Keywords: Covid19-NMR; Non-structural protein; Nucleic acid-binding domain; Protein drugability; SARS-CoV-2; Solution NMR-spectroscopy.
. 2020 Aug 8.
doi: 10.1007/s12104-020-09971-6. Online ahead of print.
[SUP]1[/SUP] H, [SUP]13[/SUP] C, and [SUP]15[/SUP] N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e
Sophie M Korn[SUP] 1 2 [/SUP], Karthikeyan Dhamotharan[SUP] 1 2 [/SUP], Boris F?rtig[SUP] 3 2 [/SUP], Martin Hengesbach[SUP] 3 2 [/SUP], Frank L?hr[SUP] 4 2 [/SUP], Nusrat S Qureshi[SUP] 3 2 [/SUP], Christian Richter[SUP] 3 2 [/SUP], Krishna Saxena[SUP] 3 2 [/SUP], Harald Schwalbe[SUP] 3 2 [/SUP], Jan-Niklas Tants[SUP] 1 2 [/SUP], Julia E Weigand[SUP] 5 [/SUP], Jens W?hnert[SUP] 1 2 [/SUP], Andreas Schlundt[SUP] 6 7 [/SUP]
Affiliations
- PMID: 32770392
- DOI: 10.1007/s12104-020-09971-6
Abstract
The ongoing pandemic caused by the Betacoronavirus SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus-2) demonstrates the urgent need of coordinated and rapid research towards inhibitors of the COVID-19 lung disease. The covid19-nmr consortium seeks to support drug development by providing publicly accessible NMR data on the viral RNA elements and proteins. The SARS-CoV-2 genome encodes for approximately 30 proteins, among them are the 16 so-called non-structural proteins (Nsps) of the replication/transcription complex. The 217-kDa large Nsp3 spans one polypeptide chain, but comprises multiple independent, yet functionally related domains including the viral papain-like protease. The Nsp3e sub-moiety contains a putative nucleic acid-binding domain (NAB) with so far unknown function and consensus target sequences, which are conceived to be both viral and host RNAs and DNAs, as well as protein-protein interactions. Its NMR-suitable size renders it an attractive object to study, both for understanding the SARS-CoV-2 architecture and drugability besides the classical virus' proteases. We here report the near-complete NMR backbone chemical shifts of the putative Nsp3e NAB that reveal the secondary structure and compactness of the domain, and provide a basis for NMR-based investigations towards understanding and interfering with RNA- and small-molecule-binding by Nsp3e.
Keywords: Covid19-NMR; Non-structural protein; Nucleic acid-binding domain; Protein drugability; SARS-CoV-2; Solution NMR-spectroscopy.