Abstract
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.
【초록키워드】 SARS-CoV-2, Coronaviruses, inhibitors, RNA, Protein, specificity, Region, N protein, Tryptophan, mutant, crystal structure, binding, nucleotide, Interaction, C-terminal domain, EMSA, biochemical, complex, residue, sequence, conformation, SARS-CoV-2 nucleocapsid, guanine, oligonucleotide, Packaging sequence, responsible, conserved, addition, facilitate, the N protein, CTD, GTP, 【제목키워드】 SARS-CoV-2, Protein, identification,