| Autor: |
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 |
| Zdroj: |
Biomolecular NMR Assignments; Oct2021, Vol. 15 Issue 2, p235-241, 7p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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