Identification of a guanine-specific pocket in the protein N of SARS-CoV-2
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The SARS-CoV-2 nucleocapsid protein (N) is responsible for RNA binding. Here we report the crystal structure of the C-terminal domain (NCTD) in open and closed conformations and in complex with guanine triphosphate, GTP. The crystal structure and biochemical studies reveal a specific interaction between the guanine, a nucleotide enriched in the packaging signals regions of coronaviruses, and a highly conserved tryptophan residue (W330). In addition, EMSA assays with SARS-CoV-2 derived RNA hairpin loops from a putative viral packaging sequence showed the preference interaction of the N-CTD to RNA oligonucleotides containing G and the loss of the specificity in the mutant W330A. Here we propose that this interaction may facilitate the viral assembly process. In summary, we have identified a specific guanine-binding pocket in the N protein that may be used to design viral assembly inhibitors.
Original language | English |
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Article number | 711 |
Journal | Communications Biology |
Volume | 5 |
Issue number | 1 |
Number of pages | 9 |
ISSN | 2399-3642 |
DOIs | |
Publication status | Published - 2022 |
Externally published | Yes |
Bibliographical note
© 2022. The Author(s).
- COVID-19, Guanine, Humans, Nucleocapsid Proteins/chemistry, RNA, Viral/metabolism, SARS-CoV-2/genetics
Research areas
ID: 314626731