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

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F22%3A00559451" target="_blank" >RIV/61388963:_____/22:00559451 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.1016/j.jsb.2022.107879" target="_blank" >https://doi.org/10.1016/j.jsb.2022.107879</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jsb.2022.107879" target="_blank" >10.1016/j.jsb.2022.107879</a>

Result language
angličtina
Original language name
Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins
Original language description
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.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology

Project
<a href="/en/project/EF16_019%2F0000729" target="_blank" >EF16_019/0000729: Chemical biology for drugging undruggable targets</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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