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dc.contributor.authorWang, Ying
dc.contributor.authorKirkpatrick, John
dc.contributor.authorZur Lage, Susanne
dc.contributor.authorKorn, Sophie M
dc.contributor.authorNeißner, Konstantin
dc.contributor.authorSchwalbe, Harald
dc.contributor.authorSchlundt, Andreas
dc.contributor.authorCarlomagno, Teresa
dc.date.accessioned2021-07-05T14:02:36Z
dc.date.available2021-07-05T14:02:36Z
dc.date.issued2021-03-26
dc.identifier.citationBiomol NMR Assign. 2021 Mar 26:1–9. doi: 10.1007/s12104-021-10019-6. Epub ahead of print.en_US
dc.identifier.pmid33770349
dc.identifier.doi10.1007/s12104-021-10019-6
dc.identifier.urihttp://hdl.handle.net/10033/622923
dc.description.abstractThe 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.isoenen_US
dc.publisherSPringeren_US
dc.rightsAttribution 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subject5′ untranslated regionen_US
dc.subjectNMR spectroscopyen_US
dc.subjectNew drug targetsen_US
dc.subjectNon-structural proteinsen_US
dc.subjectNsp1en_US
dc.subjectSARS-CoV-2en_US
dc.title1H, 13C, and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein)en_US
dc.typeArticleen_US
dc.identifier.eissn1874-270X
dc.contributor.departmentHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.en_US
dc.identifier.journalBiomolecular NMR assignmentsen_US
refterms.dateFOA2021-07-05T14:02:37Z
dc.source.journaltitleBiomolecular NMR assignments
dc.source.countryNetherlands


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Attribution 4.0 International
Except where otherwise noted, this item's license is described as Attribution 4.0 International