Research output: Contribution to journal › Article › peer-review
Erika Foldesne Dudas, Rita Puglisi, Sophie Marianne Korn, Caterina Alfano, Maria Laura Bellone, Fabrizio Dal Piaz, Geoff Kelly, Elisa Monaca, Andreas Schlundt, Harald Schwalbe, Annalisa Pastore
Original language | English |
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Pages (from-to) | 235-241 |
Number of pages | 7 |
Journal | Biomolecular NMR Assignments |
Volume | 15 |
Issue number | 2 |
DOIs | |
Published | Oct 2021 |
Additional links |
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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