| Literature DB >> 33755914 |
Erika F Dudás1, Rita Puglisi1, Sophie Marianne Korn2,3, Caterina Alfano4, Maria Laura Bellone5, Fabrizio Dal Piaz5, Geoff Kelly6, Elisa Monaca4, Andreas Schlundt2,3, Harald Schwalbe2,3, Annalisa Pastore7.
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.Entities:
Keywords: Coronavirus; Covid-19 NMR; Protein; SARS-CoV-2; Solution NMR; Structure
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Year: 2021 PMID： 33755914 PMCID： PMC7985572 DOI： 10.1007/s12104-021-10011-0
Source DB: PubMed Journal: Biomol NMR Assign ISSN： 1874-270X Impact factor: 0.746