Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins.
J Struct Biol
; 214(3): 107879, 2022 09.
Article
in English
| MEDLINE | ID: covidwho-1914725
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.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
14-3-3 Proteins
/
Coronavirus Nucleocapsid Proteins
/
SARS-CoV-2
Limits:
Humans
Language:
English
Journal:
J Struct Biol
Journal subject:
Molecular Biology
Year:
2022
Document Type:
Article
Affiliation country:
J.jsb.2022.107879
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