Abstract
The nucleocapsid (N) protein is one of the four structural proteins of the SARS-CoV-2 virus and plays a crucial role in viral genome organization and, hence, replication and pathogenicity. The N-terminal domain (N NTD ) binds to the genomic RNA and thus comprises a potential target for inhibitor and vaccine development. We determined the atomic-resolution structure of crystalline N NTD by integrating solid-state magic angle spinning (MAS) NMR and X-ray diffraction. Our combined approach provides atomic details of protein packing interfaces as well as information about flexible regions as the N- and C-termini and the functionally important RNA binding, β-hairpin loop. In addition, ultrafast (100 kHz) MAS 1 H-detected experiments permitted the assignment of side-chain proton chemical shifts not available by other means. The present structure offers guidance for designing therapeutic interventions against the SARS-CoV-2 infection.
【초록키워드】 Vaccine development, SARS-COV-2 infection, Infection, SARS-CoV-2 virus, RNA, Replication, Protein, Region, nucleocapsid, structural proteins, NTD, structural protein, experiment, pathogenicity, inhibitor, information, Guidance, NMR, binding, N-terminal domain, genomic RNA, X-ray diffraction, therapeutic interventions, therapeutic intervention, offer, genome organization, approach, means, N- and C-termini, bind, flexible, addition, provide, atomic, in viral, the SARS-CoV-2, the SARS-CoV-2 virus, 【제목키워드】 Structure, SARS-CoV-2,