3QZS

Crystal Structure of BPTF bromo in complex with histone H4K16ac - Form I

3QZS の概要

• エントリーDOI: 10.2210/pdb3qzs/pdb
• 関連するPDBエントリー: 3QZT 3QZV
• 分子名称: Nucleosome-remodeling factor subunit BPTF, Histone H4 (3 entities in total)
• 機能のキーワード: protein-peptide complex, transcription-nuclear protein complex, transcription/nuclear protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: Q12830; Nucleus: P62805
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 29137.33

構造登録者

Li, H.,Ruthenburg, A.J.,Patel, D.J. (登録日: 2011-03-07, 公開日: 2011-06-01, 最終更新日: 2024-11-20)

主引用文献

Ruthenburg, A.J.,Li, H.,Milne, T.A.,Dewell, S.,McGinty, R.K.,Yuen, M.,Ueberheide, B.,Dou, Y.,Muir, T.W.,Patel, D.J.,Allis, C.D.
Recognition of a Mononucleosomal Histone Modification Pattern by BPTF via Multivalent Interactions.
Cell(Cambridge,Mass.), 145:692-706, 2011

PubMed Abstract: Little is known about how combinations of histone marks are interpreted at the level of nucleosomes. The second PHD finger of human BPTF is known to specifically recognize histone H3 when methylated on lysine 4 (H3K4me2/3). Here, we examine how additional heterotypic modifications influence BPTF binding. Using peptide surrogates, three acetyllysine ligands are indentified for a PHD-adjacent bromodomain in BPTF via systematic screening and biophysical characterization. Although the bromodomain displays limited discrimination among the three possible acetyllysines at the peptide level, marked selectivity is observed for only one of these sites, H4K16ac, in combination with H3K4me3 at the mononucleosome level. In support, these two histone marks constitute a unique trans-histone modification pattern that unambiguously resides within a single nucleosomal unit in human cells, and this module colocalizes with these marks in the genome. Together, our data call attention to nucleosomal patterning of covalent marks in dictating critical chromatin associations.

PubMed: 21596426
DOI: 10.1016/j.cell.2011.03.053

実験手法

X-RAY DIFFRACTION (1.8 Å)