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Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9.


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.

SUBMITTER: F Dudas E 

PROVIDER: S-EPMC7985572 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature

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Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9.

F Dudás Erika E   Puglisi Rita R   Korn Sophie Marianne SM   Alfano Caterina C   Bellone Maria Laura ML   Piaz Fabrizio Dal FD   Kelly Geoff G   Monaca Elisa E   Schlundt Andreas A   Schwalbe Harald H   Pastore Annalisa A  

Biomolecular NMR assignments 20210323 2


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 an  ...[more]

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