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Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins.

ABSTRACT: 14-3-3 proteins are important dimeric scaffolds that regulate the function of hundreds of proteins in a phosphorylation-dependent manner. The SARS-CoV-2 nucleocapsid (N) protein forms a complex with human 14-3-3 proteins upon phosphorylation, which has also been described for other coronaviruses. Here, we report a high-resolution crystal structure of 14-3-3 bound to an N phosphopeptide bearing the phosphoserine 197 in the middle. The structure revealed two copies of the N phosphopeptide bound, each in the central binding groove of each 14-3-3 monomer. A complex network of hydrogen bonds and water bridges between the peptide and 14-3-3 was observed explaining the high affinity of the N protein for 14-3-3 proteins.

SUBMITTER: Eisenreichova A

PROVIDER: S-EPMC9245327 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature

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Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins.

Eisenreichova Andrea A Boura Evzen E

Journal of structural biology 20220630 3

14-3-3 proteins are important dimeric scaffolds that regulate the function of hundreds of proteins in a phosphorylation-dependent manner. The SARS-CoV-2 nucleocapsid (N) protein forms a complex with human 14-3-3 proteins upon phosphorylation, which has also been described for other coronaviruses. Here, we report a high-resolution crystal structure of 14-3-3 bound to an N phosphopeptide bearing the phosphoserine 197 in the middle. The structure revealed two copies of the N phosphopeptide bound, e ...[more]

PMID: 35781025

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