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Pustovalova Y, Gorbatyuk O, Li Y, et al. Backbone and Ile, Leu, Val methyl group resonance assignment of CoV-Y domain of SARS-CoV-2 non-structural protein 3. Biomol NMR Assign. 2021;doi: 10.1007/s12104-021-10059-y.
Pustovalova, Y., Gorbatyuk, O., Li, Y., Hao, B., & Hoch, J. C. (2021). Backbone and Ile, Leu, Val methyl group resonance assignment of CoV-Y domain of SARS-CoV-2 non-structural protein 3. Biomolecular NMR assignments, . https://doi.org/10.1007/s12104-021-10059-y
Pustovalova, Yulia, et al. "Backbone and Ile, Leu, Val methyl group resonance assignment of CoV-Y domain of SARS-CoV-2 non-structural protein 3." Biomolecular NMR assignments vol. (2021). doi: https://doi.org/10.1007/s12104-021-10059-y
Pustovalova Y, Gorbatyuk O, Li Y, Hao B, Hoch JC. Backbone and Ile, Leu, Val methyl group resonance assignment of CoV-Y domain of SARS-CoV-2 non-structural protein 3. Biomol NMR Assign. 2021 Nov 18; doi: 10.1007/s12104-021-10059-y. Epub 2021 Nov 18. PMID: 34792756; PMCID: PMC8600339.
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Biomol NMR Assign. 2021 Nov 18; doi: 10.1007/s12104-021-10059-y. Epub 2021 Nov 18.

Backbone and Ile, Leu, Val methyl group resonance assignment of CoV-Y domain of SARS-CoV-2 non-structural protein 3.

Biomolecular NMR assignments

Yulia Pustovalova, Oksana Gorbatyuk, Yunfeng Li, Bing Hao, Jeffrey C Hoch

Affiliations

  1. Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT, 06030, USA. [email protected].
  2. Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT, 06030, USA.
  3. Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT, 06030, USA. [email protected].

PMID: 34792756 PMCID: PMC8600339 DOI: 10.1007/s12104-021-10059-y

Abstract

The worldwide COVID-19 pandemic is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Nonstructural protein 3 (nsp3) has 1945 residues and is the largest protein encoded by SARS-CoV-2. It comprises more than a dozen independent domains with various functions. Many of these domains were studied in the closely-related virus SARS-CoV following an earlier outbreak. Nonetheless structural and functional information on the C-terminal region of nsp3 containing two transmembrane and three extra-membrane domains remains incomplete. This part of the protein appears to be involved in initiation of double membrane vesicle (DMV) formation, membranous organelles the virus builds to hide its replication-transcription complex from host immune defenses. Here we present the near-complete backbone and Ile, Leu, and Val methyl group chemical shift assignments of the most C-terminal domain of nsp3, CoV-Y. As the exact function and binding partners of CoV-Y remain unknown, our data provide a basis for future NMR studies of protein-protein interactions to elucidate the molecular mechanism of DMV formation.

© 2021. The Author(s), under exclusive licence to Springer Nature B.V.

Keywords: CoV-Y domain; Methyl assignment; SARS-CoV-2; nsp3

References

  1. J Biomol NMR. 2004 Feb;28(2):165-72 - PubMed
  2. Science. 2020 Sep 11;369(6509):1395-1398 - PubMed
  3. J Biomol NMR. 2017 Jun;68(2):101-118 - PubMed
  4. J Am Chem Soc. 2005 Mar 2;127(8):2767-75 - PubMed
  5. Antiviral Res. 2018 Jan;149:58-74 - PubMed
  6. J Am Chem Soc. 2003 Nov 12;125(45):13868-78 - PubMed
  7. Proteins. 2005 Jun 1;59(4):687-96 - PubMed
  8. Virus Res. 2008 May;133(2):136-48 - PubMed
  9. Antiviral Res. 2016 Nov;135:97-107 - PubMed
  10. J Biomol NMR. 1994 Nov;4(6):845-58 - PubMed
  11. mBio. 2013 Aug 13;4(4): - PubMed
  12. J Biomol NMR. 1995 Nov;6(3):277-93 - PubMed
  13. Curr Opin Microbiol. 2016 Aug;32:82-88 - PubMed
  14. Virology. 2014 Jun;458-459:125-35 - PubMed
  15. Front Mol Biosci. 2021 May 10;8:653148 - PubMed
  16. Methods Mol Biol. 2015;1260:17-32 - PubMed

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