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1H, 13C, and 15N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e.
Korn, Sophie M; Dhamotharan, Karthikeyan; Fürtig, Boris; Hengesbach, Martin; Löhr, Frank; Qureshi, Nusrat S; Richter, Christian; Saxena, Krishna; Schwalbe, Harald; Tants, Jan-Niklas; Weigand, Julia E; Wöhnert, Jens; Schlundt, Andreas.
  • Korn SM; Institute for Molecular Biosciences, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 9, 60438, Frankfurt, Germany.
  • Dhamotharan K; Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, 60438, Frankfurt, Germany.
  • Fürtig B; Institute for Molecular Biosciences, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 9, 60438, Frankfurt, Germany.
  • Hengesbach M; Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, 60438, Frankfurt, Germany.
  • Löhr F; Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438, Frankfurt, Germany.
  • Qureshi NS; Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, 60438, Frankfurt, Germany.
  • Richter C; Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438, Frankfurt, Germany.
  • Saxena K; Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, 60438, Frankfurt, Germany.
  • Schwalbe H; Institute of Biophysical Chemistry, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 9, 60438, Frankfurt, Germany.
  • Tants JN; Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, 60438, Frankfurt, Germany.
  • Weigand JE; Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438, Frankfurt, Germany.
  • Wöhnert J; Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, 60438, Frankfurt, Germany.
  • Schlundt A; Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438, Frankfurt, Germany.
Biomol NMR Assign ; 14(2): 329-333, 2020 10.
Article in English | MEDLINE | ID: covidwho-774089
Semantic information from SemMedBD (by NLM)
1. Evaluation procedure USES Magnetic Resonance Imaging
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Evaluation procedure
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USES
Object
Magnetic Resonance Imaging
2. Evaluation procedure USES Magnetic Resonance Imaging
Subject
Evaluation procedure
Predicate
USES
Object
Magnetic Resonance Imaging
ABSTRACT
The ongoing pandemic caused by the Betacoronavirus SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus-2) demonstrates the urgent need of coordinated and rapid research towards inhibitors of the 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 encodes for approximately 30 proteins, among them are the 16 so-called non-structural proteins (Nsps) of the replication/transcription complex. The 217-kDa large Nsp3 spans one polypeptide chain, but comprises multiple independent, yet functionally related domains including the viral papain-like protease. The Nsp3e sub-moiety contains a putative nucleic acid-binding domain (NAB) with so far unknown function and consensus target sequences, which are conceived to be both viral and host RNAs and DNAs, as well as protein-protein interactions. Its NMR-suitable size renders it an attractive object to study, both for understanding the SARS-CoV-2 architecture and drugability besides the classical virus' proteases. We here report the near-complete NMR backbone chemical shifts of the putative Nsp3e NAB that reveal the secondary structure and compactness of the domain, and provide a basis for NMR-based investigations towards understanding and interfering with RNA- and small-molecule-binding by Nsp3e.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Nucleic Acids / Viral Nonstructural Proteins / Carbon-13 Magnetic Resonance Spectroscopy / Proton Magnetic Resonance Spectroscopy / Betacoronavirus / Nitrogen Isotopes Language: English Journal: Biomol NMR Assign Journal subject: Molecular Biology / Nuclear Medicine Year: 2020 Document Type: Article Affiliation country: S12104-020-09971-6

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Nucleic Acids / Viral Nonstructural Proteins / Carbon-13 Magnetic Resonance Spectroscopy / Proton Magnetic Resonance Spectroscopy / Betacoronavirus / Nitrogen Isotopes Language: English Journal: Biomol NMR Assign Journal subject: Molecular Biology / Nuclear Medicine Year: 2020 Document Type: Article Affiliation country: S12104-020-09971-6