Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9
| Autor: | Andreas Schlundt, Erika F. Dudás, Harald Schwalbe, Caterina Alfano, Elisa Monaca, Annalisa Pastore, Rita Puglisi, Maria Laura Bellone, Geoff Kelly, Fabrizio Dal Piaz, Sophie Marianne Korn |
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| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Stereochemistry viruses Crystal structure Viral Nonstructural Proteins 010402 general chemistry medicine.disease_cause 01 natural sciences Biochemistry Protein Structure Secondary Article Virus Imaging Analytical Ultracentrifugation 03 medical and health sciences Dynamic light scattering Structural Biology medicine Nuclear Magnetic Resonance Biomolecular 030304 developmental biology Coronavirus Solution NMR 0303 health sciences SARS-CoV-2 Chemistry Protein RNA-Binding Proteins Covid-19 NMR Structure RNA Hydrogen-Ion Concentration Small molecule 3. Good health 0104 chemical sciences Viral replication Structural Biology & Biophysics |
| Zdroj: | Biomolecular Nmr Assignments |
| DOI: | 10.25418/crick.16708711 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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