7ZIT

14-3-3 in complex with SARS-COV2 N phospho-peptide

Summary for 7ZIT

Entry DOI	10.2210/pdb7zit/pdb
Descriptor	14-3-3 protein zeta/delta, Nucleoprotein, ACETATE ION, ... (6 entities in total)
Functional Keywords	covid, coronavirus, n-phosphopeptide, protein binding
Biological source	Homo sapiens (human) More
Total number of polymer chains	4
Total formula weight	54563.26
Authors	Eisenreichova, A.,Boura, E. (deposition date: 2022-04-08, release date: 2022-10-26, Last modification date: 2024-10-23)
Primary citation	Eisenreichova, A.,Boura, E. Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins. J.Struct.Biol., 214:107879-107879, 2022 Cited by PubMed 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. PubMed: 35781025 DOI: 10.1016/j.jsb.2022.107879 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.79 Å)

Structure validation