tetano
Editor, Senior Moderator
Biomol NMR Assign
. 2021 Mar 23;1-7.
doi: 10.1007/s12104-021-10011-0. Online ahead of print.
Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9
Erika F Dud?s[SUP] #[/SUP][SUP] 1 [/SUP], Rita Puglisi[SUP] #[/SUP][SUP] 1 [/SUP], Sophie Marianne Korn[SUP] 2 3 [/SUP], Caterina Alfano[SUP] 4 [/SUP], Maria Laura Bellone[SUP] 5 [/SUP], Fabrizio Dal Piaz[SUP] 5 [/SUP], Geoff Kelly[SUP] 6 [/SUP], Elisa Monaca[SUP] 4 [/SUP], Andreas Schlundt[SUP] 2 3 [/SUP], Harald Schwalbe[SUP] 2 3 [/SUP], Annalisa Pastore[SUP] 7 [/SUP]
Affiliations
Abstract
As part of an International consortium aiming at the characterization by NMR of the proteins of the SARS-CoV-2 virus, we have obtained the virtually complete assignment of the backbone atoms of the non-structural protein nsp9. This small (12 kDa) protein is encoded by ORF1a, binds to RNA and seems to be essential for viral RNA synthesis. The crystal structures of the SARS-CoV-2 protein and other homologues suggest that the protein is dimeric as also confirmed by analytical ultracentrifugation and dynamic light scattering. Our data constitute the prerequisite for further NMR-based characterization, and provide the starting point for the identification of small molecule lead compounds that could interfere with RNA binding and prevent viral replication.
Keywords: Coronavirus; Covid-19 NMR; Protein; SARS-CoV-2; Solution NMR; Structure.
. 2021 Mar 23;1-7.
doi: 10.1007/s12104-021-10011-0. Online ahead of print.
Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9
Erika F Dud?s[SUP] #[/SUP][SUP] 1 [/SUP], Rita Puglisi[SUP] #[/SUP][SUP] 1 [/SUP], Sophie Marianne Korn[SUP] 2 3 [/SUP], Caterina Alfano[SUP] 4 [/SUP], Maria Laura Bellone[SUP] 5 [/SUP], Fabrizio Dal Piaz[SUP] 5 [/SUP], Geoff Kelly[SUP] 6 [/SUP], Elisa Monaca[SUP] 4 [/SUP], Andreas Schlundt[SUP] 2 3 [/SUP], Harald Schwalbe[SUP] 2 3 [/SUP], Annalisa Pastore[SUP] 7 [/SUP]
Affiliations
- PMID: 33755914
- PMCID: PMC7985572
- DOI: 10.1007/s12104-021-10011-0
Abstract
As part of an International consortium aiming at the characterization by NMR of the proteins of the SARS-CoV-2 virus, we have obtained the virtually complete assignment of the backbone atoms of the non-structural protein nsp9. This small (12 kDa) protein is encoded by ORF1a, binds to RNA and seems to be essential for viral RNA synthesis. The crystal structures of the SARS-CoV-2 protein and other homologues suggest that the protein is dimeric as also confirmed by analytical ultracentrifugation and dynamic light scattering. Our data constitute the prerequisite for further NMR-based characterization, and provide the starting point for the identification of small molecule lead compounds that could interfere with RNA binding and prevent viral replication.
Keywords: Coronavirus; Covid-19 NMR; Protein; SARS-CoV-2; Solution NMR; Structure.