دورية أكاديمية
1H, 13C, and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein)
| العنوان: | 1H, 13C, and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein) |
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| المؤلفون: | Wang, Ying, Kirkpatrick, John, Lage, Susanne zur, Korn, Sophie M., Neißner, Konstantin, Schwalbe, Harald, Schlundt, Andreas, Carlomagno, Teresa |
| المصدر: | Biomolecular NMR Assignments 15 (2021), Nr. 2 ; Biomolecular NMR Assignments |
| بيانات النشر: | Springer Netherlands |
| سنة النشر: | 2021 |
| المجموعة: | Institutional Repository of Leibniz Universität Hannover |
| مصطلحات موضوعية: | 5′ untranslated region, New drug targets, NMR spectroscopy, Non-structural proteins, Nsp1, viral protein, chemistry, molecular model, nuclear magnetic resonance, protein domain, Models, Molecular, Biomolecular, Protein Domains, SARS-CoV-2, Viral Nonstructural Proteins, ddc:570 |
| الوصف: | 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. © 2021, The Author(s). |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | ESSN:1874-270X; http://dx.doi.org/10.15488/12342Test; https://www.repo.uni-hannover.de/handle/123456789/12441Test |
| DOI: | 10.15488/12342 |
| الإتاحة: | https://doi.org/10.15488/12342Test https://doi.org/10.1007/s12104-021-10019-6Test https://www.repo.uni-hannover.de/handle/123456789/12441Test |
| حقوق: | CC BY 4.0 Unported ; https://creativecommons.org/licenses/by/4.0Test/ ; frei zugänglich |
| رقم الانضمام: | edsbas.26034DB5 |
| قاعدة البيانات: | BASE |
| DOI: | 10.15488/12342 |
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