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Publication Abstract from PubMed

The SARS-CoV-2 nucleocapsid protein (N) is responsible for RNA binding. Here we report the crystal structure of the C-terminal domain (N(CTD)) 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.

Identification of a guanine-specific pocket in the protein N of SARS-CoV-2.,Rafael Ciges-Tomas J, Franco ML, Vilar M Commun Biol. 2022 Jul 16;5(1):711. doi: 10.1038/s42003-022-03647-8. PMID:35842466^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.