dc.identifier.uri |
http://dx.doi.org/10.15488/12342 |
|
dc.identifier.uri |
https://www.repo.uni-hannover.de/handle/123456789/12441 |
|
dc.contributor.author |
Wang, Ying
|
|
dc.contributor.author |
Kirkpatrick, John
|
|
dc.contributor.author |
Lage, Susanne zur
|
|
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 |
2022-06-27T04:36:59Z |
|
dc.date.available |
2022-06-27T04:36:59Z |
|
dc.date.issued |
2021 |
|
dc.identifier.citation |
Wang, Y.; Kirkpatrick, J.; Lage, S. zur; Korn, S.M.; Neißner, K. et al.: 1H, 13C, and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein). In: Biomolecular NMR Assignments 15 (2021), Nr. 2, S. 287-295. DOI: https://doi.org/10.1007/s12104-021-10019-6 |
|
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. © 2021, The Author(s). |
eng |
dc.language.iso |
eng |
|
dc.publisher |
Dordrecht [u.a.] : Springer Netherlands |
|
dc.relation.ispartofseries |
Biomolecular NMR Assignments 15 (2021), Nr. 2 |
|
dc.rights |
CC BY 4.0 Unported |
|
dc.rights.uri |
https://creativecommons.org/licenses/by/4.0/ |
|
dc.subject |
5′ untranslated region |
eng |
dc.subject |
New drug targets |
eng |
dc.subject |
NMR spectroscopy |
eng |
dc.subject |
Non-structural proteins |
eng |
dc.subject |
Nsp1 |
eng |
dc.subject |
viral protein |
eng |
dc.subject |
chemistry |
eng |
dc.subject |
molecular model |
eng |
dc.subject |
nuclear magnetic resonance |
eng |
dc.subject |
protein domain |
eng |
dc.subject |
Models, Molecular |
eng |
dc.subject |
Nuclear Magnetic Resonance, Biomolecular |
eng |
dc.subject |
Protein Domains |
eng |
dc.subject |
SARS-CoV-2 |
eng |
dc.subject |
Viral Nonstructural Proteins |
eng |
dc.subject.ddc |
570 | Biowissenschaften, Biologie
|
ger |
dc.title |
1H, 13C, and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein) |
|
dc.type |
Article |
|
dc.type |
Text |
|
dc.relation.essn |
1874-270X |
|
dc.relation.doi |
https://doi.org/10.1007/s12104-021-10019-6 |
|
dc.bibliographicCitation.issue |
2 |
|
dc.bibliographicCitation.volume |
15 |
|
dc.bibliographicCitation.firstPage |
287 |
|
dc.bibliographicCitation.lastPage |
295 |
|
dc.description.version |
publishedVersion |
|
tib.accessRights |
frei zug�nglich |
|