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

0559451 - ÚOCHB 2023 RIV US eng J - Článek v odborném periodiku
Eisenreichová, Andrea - Bouřa, Evžen
Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins.
Journal of Structural Biology. Roč. 214, č. 3 (2022), č. článku 107879. ISSN 1047-8477. E-ISSN 1095-8657
Grant CEP: GA MŠMT(CZ) EF16_019/0000729
Institucionální podpora: RVO:61388963
Klíčová slova: binding * motif
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 3, rok: 2022
Způsob publikování: Omezený přístup
https://doi.org/10.1016/j.jsb.2022.107879

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.
Trvalý link: https://hdl.handle.net/11104/0332747


Vědecká data: Worldwide PDB