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Atomic-Resolution Structure of SARS-CoV-2 Nucleocapsid Protein N-Terminal Domain.

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 (NNTD) binds to the genomic RNA and thus comprises a potential target for inhibitor and vaccine development. We determined the atomic-resolution structure of crystalline NNTD 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 1H-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.

SUBMITTER: Sarkar S 

PROVIDER: S-EPMC9173677 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature

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Atomic-Resolution Structure of SARS-CoV-2 Nucleocapsid Protein N-Terminal Domain.

Sarkar Sucharita S   Runge Brent B   Russell Ryan W RW   Movellan Kumar Tekwani KT   Calero Daniel D   Zeinalilathori Somayeh S   Quinn Caitlin M CM   Lu Manman M   Calero Guillermo G   Gronenborn Angela M AM   Polenova Tatyana T  

Journal of the American Chemical Society 20220531 23

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<sup>NTD</sup>) 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<sup>NTD</sup> by integrating solid-state magic angle spinning (MAS) NMR and X-ray diffraction. Our combine  ...[more]

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