1H, 13C, and 15N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e.
Biomol NMR Assign
; 14(2): 329-333, 2020 10.
Article
em En
| MEDLINE
| ID: mdl-32770392
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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Temas:
Geral
Base de dados:
MEDLINE
Assunto principal:
Ácidos Nucleicos
/
Proteínas não Estruturais Virais
/
Espectroscopia de Ressonância Magnética Nuclear de Carbono-13
/
Espectroscopia de Prótons por Ressonância Magnética
/
Betacoronavirus
/
Isótopos de Nitrogênio
Idioma:
En
Revista:
Biomol NMR Assign
Assunto da revista:
BIOLOGIA MOLECULAR
/
MEDICINA NUCLEAR
Ano de publicação:
2020
Tipo de documento:
Article
País de afiliação:
Alemanha