Your browser doesn't support javascript.
Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins.
Eisenreichova, Andrea; Boura, Evzen.
  • Eisenreichova A; Institute of Organic Chemistry and Biochemistry AS CR, v.v.i., Flemingovo nam. 2, 166 10 Prague 6, Czech Republic.
  • Boura E; Institute of Organic Chemistry and Biochemistry AS CR, v.v.i., Flemingovo nam. 2, 166 10 Prague 6, Czech Republic. Electronic address: boura@uochb.cas.cz.
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.
Subject(s)

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

Similar

MEDLINE

...
LILACS

LIS


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