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Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins
A. Eisenreichova, E. Boura
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články
- MeSH
- COVID-19 MeSH
- fosfopeptidy chemie MeSH
- fosfoproteiny chemie MeSH
- koronavirové nukleokapsidové proteiny * chemie MeSH
- lidé MeSH
- proteiny 14-3-3 * chemie MeSH
- SARS-CoV-2 * MeSH
- vazba proteinů MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
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.
Citace poskytuje Crossref.org
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