2X35

Molecular basis of Histone H3K36me3 recognition by the PWWP domain of BRPF1.

2X35 の概要

• エントリーDOI: 10.2210/pdb2x35/pdb
• 関連するPDBエントリー: 2D9E
• 分子名称: PEREGRIN (2 entities in total)
• 機能のキーワード: transcription, metal-binding, zinc-finger, dna-binding, chromatin regulator, transcription regulation, nucleosome
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Nucleus : P55201
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15249.58

構造登録者

Vezzoli, A.,Bonadies, N.,Allen, M.D.,Freund, S.M.V.,Santiveri, C.M.,Kvinlaug, B.,Huntly, B.J.P.,Gottgens, B.,Bycroft, M. (登録日: 2010-01-21, 公開日: 2010-02-02, 最終更新日: 2024-05-08)

主引用文献

Vezzoli, A.,Bonadies, N.,Allen, M.D.,Freund, S.M.V.,Santiveri, C.M.,Kvinlaug, B.,Huntly, B.J.P.,Gottgens, B.,Bycroft, M.
Molecular Basis of Histone H3K36Me3 Recognition by the Pwwp Domain of Brpf1.
Nat.Struct.Mol.Biol., 17:617-, 2010

PubMed Abstract: Trimethylation of Lys36 in histone H3 (H3K36me3) coordinates events associated with the elongation phase of transcription and is also emerging as an important epigenetic regulator of cell growth and differentiation. We have identified the PWWP domain of bromo and plant homeodomain (PHD) finger-containing protein 1 (BRPF1) as a H3K36me3 binding module and have determined the structure of this domain in complex with an H3K36me3-derived peptide.

PubMed: 20400950
DOI: 10.1038/NSMB.1797

実験手法

X-RAY DIFFRACTION (2 Å)