7ZIT

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

7ZIT の概要

• エントリーDOI: 10.2210/pdb7zit/pdb
• 分子名称: 14-3-3 protein zeta/delta, Nucleoprotein, ACETATE ION, ... (6 entities in total)
• 機能のキーワード: covid, coronavirus, n-phosphopeptide, protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 54563.26

構造登録者

Eisenreichova, A.,Boura, E. (登録日: 2022-04-08, 公開日: 2022-10-26, 最終更新日: 2024-10-23)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.79 Å)