1H, 13C, and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein)
dc.contributor.author | Wang, Ying | |
dc.contributor.author | Kirkpatrick, John | |
dc.contributor.author | Zur Lage, Susanne | |
dc.contributor.author | Korn, Sophie M | |
dc.contributor.author | Neißner, Konstantin | |
dc.contributor.author | Schwalbe, Harald | |
dc.contributor.author | Schlundt, Andreas | |
dc.contributor.author | Carlomagno, Teresa | |
dc.date.accessioned | 2021-07-05T14:02:36Z | |
dc.date.available | 2021-07-05T14:02:36Z | |
dc.date.issued | 2021-03-26 | |
dc.identifier.citation | Biomol NMR Assign. 2021 Mar 26:1–9. doi: 10.1007/s12104-021-10019-6. Epub ahead of print. | en_US |
dc.identifier.pmid | 33770349 | |
dc.identifier.doi | 10.1007/s12104-021-10019-6 | |
dc.identifier.uri | http://hdl.handle.net/10033/622923 | |
dc.description.abstract | The current COVID-19 pandemic caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has become a worldwide health crisis, necessitating coordinated scientific research and urgent identification of new drug targets for treatment of 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 comprises a single RNA of about 30 kb in length, in which 14 open reading frames (ORFs) have been annotated, and encodes approximately 30 proteins. The first two-thirds of the SARS-CoV-2 genome is made up of two large overlapping open-reading-frames (ORF1a and ORF1b) encoding a replicase polyprotein, which is subsequently cleaved to yield 16 so-called non-structural proteins. The non-structural protein 1 (Nsp1), which is considered to be a major virulence factor, suppresses host immune functions by associating with host ribosomal complexes at the very end of its C-terminus. Furthermore, Nsp1 facilitates initiation of viral RNA translation via an interaction of its N-terminal domain with the 5' untranslated region (UTR) of the viral RNA. Here, we report the near-complete backbone chemical-shift assignments of full-length SARS-CoV-2 Nsp1 (19.8 kDa), which reveal the domain organization, secondary structure and backbone dynamics of Nsp1, and which will be of value to further NMR-based investigations of both the biochemical and physiological functions of Nsp1. | en_US |
dc.language.iso | en | en_US |
dc.publisher | SPringer | en_US |
dc.rights | Attribution 4.0 International | * |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | * |
dc.subject | 5′ untranslated region | en_US |
dc.subject | NMR spectroscopy | en_US |
dc.subject | New drug targets | en_US |
dc.subject | Non-structural proteins | en_US |
dc.subject | Nsp1 | en_US |
dc.subject | SARS-CoV-2 | en_US |
dc.title | 1H, 13C, and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein) | en_US |
dc.type | Article | en_US |
dc.identifier.eissn | 1874-270X | |
dc.contributor.department | HZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany. | en_US |
dc.identifier.journal | Biomolecular NMR assignments | en_US |
refterms.dateFOA | 2021-07-05T14:02:37Z | |
dc.source.journaltitle | Biomolecular NMR assignments | |
dc.source.country | Netherlands |