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Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9.
F Dudás, Erika; Puglisi, Rita; Korn, Sophie Marianne; Alfano, Caterina; Bellone, Maria Laura; Piaz, Fabrizio Dal; Kelly, Geoff; Monaca, Elisa; Schlundt, Andreas; Schwalbe, Harald; Pastore, Annalisa.
  • F Dudás E; Department of Basic and Clinical Neuroscience, Maurice Wohl Institute, UK-DRI at King's College London, 5 Cutcombe Rd, London, SE59RT, UK.
  • Puglisi R; Department of Basic and Clinical Neuroscience, Maurice Wohl Institute, UK-DRI at King's College London, 5 Cutcombe Rd, London, SE59RT, UK.
  • Korn SM; Institute for Molecular Biosciences, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 9, 60438, Frankfurt/M, Germany.
  • Alfano C; Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438, Frankfurt/M, Germany.
  • Bellone ML; Fondazione Ri.Med, 90133, Palermo, Italy.
  • Piaz FD; Department of Medicine and Surgery, University of Salerno, Via Giovanni Paolo II, 84081, Baronissi, SA, Italy.
  • Kelly G; Department of Medicine and Surgery, University of Salerno, Via Giovanni Paolo II, 84081, Baronissi, SA, Italy.
  • Monaca E; Francis Crick Institute, MRC Biomedical NMR Centre, 1 Midland Rd, London, NW1 1AT, UK.
  • Schlundt A; Fondazione Ri.Med, 90133, Palermo, Italy.
  • Schwalbe H; Institute for Molecular Biosciences, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 9, 60438, Frankfurt/M, Germany.
  • Pastore A; Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438, Frankfurt/M, Germany.
Biomol NMR Assign ; 15(2): 235-241, 2021 10.
Article in English | MEDLINE | ID: covidwho-1146127
ABSTRACT
As part of an International consortium aiming at the characterization by NMR of the proteins of the SARS-CoV-2 virus, we have obtained the virtually complete assignment of the backbone atoms of the non-structural protein nsp9. This small (12 kDa) protein is encoded by ORF1a, binds to RNA and seems to be essential for viral RNA synthesis. The crystal structures of the SARS-CoV-2 protein and other homologues suggest that the protein is dimeric as also confirmed by analytical ultracentrifugation and dynamic light scattering. Our data constitute the prerequisite for further NMR-based characterization, and provide the starting point for the identification of small molecule lead compounds that could interfere with RNA binding and prevent viral replication.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: RNA-Binding Proteins / Viral Nonstructural Proteins / Nuclear Magnetic Resonance, Biomolecular Language: English Journal: Biomol NMR Assign Journal subject: Molecular Biology / Nuclear Medicine Year: 2021 Document Type: Article Affiliation country: S12104-021-10011-0

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Full text: Available Collection: International databases Database: MEDLINE Main subject: RNA-Binding Proteins / Viral Nonstructural Proteins / Nuclear Magnetic Resonance, Biomolecular Language: English Journal: Biomol NMR Assign Journal subject: Molecular Biology / Nuclear Medicine Year: 2021 Document Type: Article Affiliation country: S12104-021-10011-0