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2C1N

Molecular basis for the recognition of phosphorylated and phosphoacetylated histone H3 by 14-3-3

2C1N の概要
エントリーDOI10.2210/pdb2c1n/pdb
関連するPDBエントリー1IB1 1QJA 1QJB 2C1J
分子名称14-3-3 PROTEIN ZETA/DELTA, HISTONE H3 ACETYLPHOSPHOPEPTIDE (3 entities in total)
機能のキーワードsignaling protein-complex, histone h3, nucleosome, signaling protein
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60371.17
構造登録者
主引用文献Macdonald, N.,Welburn, J.P.I.,Noble, M.E.M.,Nguyen, A.,Yaffe, M.B.,Clynes, D.,Moggs, J.G.,Orphanides, G.,Thomson, S.,Edmunds, J.W.,Clayton, A.L.,Endicott, J.A.,Mahadevan, L.C.
Molecular Basis for the Recognition of Phosphorylated and Phosphoacetylated Histone H3 by 14-3-3.
Mol.Cell, 20:199-, 2005
Cited by
PubMed Abstract: Phosphorylation of histone H3 is implicated in transcriptional activation and chromosome condensation, but its immediate molecular function has remained obscure. By affinity chromatography of nuclear extracts against modified H3 tail peptides, we identified 14-3-3 isoforms as proteins that bind these tails in a strictly phosphorylation-dependent manner. Acetylation of lysines 9 and 14 does not impede 14-3-3 binding to serine 10-phosphorylated H3 tails. In vivo, 14-3-3 is inducibly recruited to c-fos and c-jun nucleosomes upon gene activation, concomitant with H3 phosphoacetylation. We have determined the structures of 14-3-3zeta complexed with serine 10-phosphorylated or phosphoacetylated H3 peptides. These reveal a distinct mode of 14-3-3/phosphopeptide binding and provide a structural understanding for the lack of effect of acetylation at lysines 9 and 14 on this interaction. 14-3-3 isoforms thus represent a class of proteins that mediate the effect of histone phosphorylation at inducible genes.
PubMed: 16246723
DOI: 10.1016/J.MOLCEL.2005.08.032
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 2c1n
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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