6ZFG
14-3-3 zeta chimera with 18E6 and fusicoccin
6ZFG の概要
エントリーDOI | 10.2210/pdb6zfg/pdb |
関連するPDBエントリー | 6ZFD |
分子名称 | 14-3-3 protein zeta/delta,Protein E6, GLYCEROL, FUSICOCCIN, ... (4 entities in total) |
機能のキーワード | 14-3-3, hpv, e6 oncoprotein, protein binding |
由来する生物種 | Homo sapiens (Human) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 56243.27 |
構造登録者 | Gogl, G.,Tugaeva, K.,Sluchanko, N.N.,Trave, G. (登録日: 2020-06-17, 公開日: 2021-02-17, 最終更新日: 2024-10-23) |
主引用文献 | Gogl, G.,Tugaeva, K.V.,Eberling, P.,Kostmann, C.,Trave, G.,Sluchanko, N.N. Hierarchized phosphotarget binding by the seven human 14-3-3 isoforms. Nat Commun, 12:1677-1677, 2021 Cited by PubMed Abstract: The seven 14-3-3 isoforms are highly abundant human proteins encoded by similar yet distinct genes. 14-3-3 proteins recognize phosphorylated motifs within numerous human and viral proteins. Here, we analyze by X-ray crystallography, fluorescence polarization, mutagenesis and fusicoccin-mediated modulation the structural basis and druggability of 14-3-3 binding to four E6 oncoproteins of tumorigenic human papillomaviruses. 14-3-3 isoforms bind variant and mutated phospho-motifs of E6 and unrelated protein RSK1 with different affinities, albeit following an ordered affinity ranking with conserved relative K ratios. Remarkably, 14-3-3 isoforms obey the same hierarchy when binding to most of their established targets, as supported by literature and a recent human complexome map. This knowledge allows predicting proportions of 14-3-3 isoforms engaged with phosphoproteins in various tissues. Notwithstanding their individual functions, cellular concentrations of 14-3-3 may be collectively adjusted to buffer the strongest phosphorylation outbursts, explaining their expression variations in different tissues and tumors. PubMed: 33723253DOI: 10.1038/s41467-021-21908-8 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.85 Å) |
構造検証レポート
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