5SZB
Structure of human Dpf3 double-PHD domain bound to histone H3 tail peptide with acetylated K14
5SZB の概要
エントリーDOI | 10.2210/pdb5szb/pdb |
関連するPDBエントリー | 5SZC |
分子名称 | Zinc finger protein DPF3, Histone H3 tail peptide, ZINC ION, ... (5 entities in total) |
機能のキーワード | chromatin, modified histone, phd domain, zinc binding domain, baf45, baf complex, peptide-binding protein, peptide binding protein |
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 | 15251.78 |
構造登録者 | Singh, N.,Local, A.,Shiau, A.,Ren, B.,Corbett, K.D. (登録日: 2016-08-13, 公開日: 2017-08-16, 最終更新日: 2024-10-09) |
主引用文献 | Local, A.,Huang, H.,Albuquerque, C.P.,Singh, N.,Lee, A.Y.,Wang, W.,Wang, C.,Hsia, J.E.,Shiau, A.K.,Ge, K.,Corbett, K.D.,Wang, D.,Zhou, H.,Ren, B. Identification of H3K4me1-associated proteins at mammalian enhancers. Nat. Genet., 50:73-82, 2018 Cited by PubMed Abstract: Enhancers act to regulate cell-type-specific gene expression by facilitating the transcription of target genes. In mammalian cells, active or primed enhancers are commonly marked by monomethylation of histone H3 at lysine 4 (H3K4me1) in a cell-type-specific manner. Whether and how this histone modification regulates enhancer-dependent transcription programs in mammals is unclear. In this study, we conducted SILAC mass spectrometry experiments with mononucleosomes and identified multiple H3K4me1-associated proteins, including many involved in chromatin remodeling. We demonstrate that H3K4me1 augments association of the chromatin-remodeling complex BAF to enhancers in vivo and that, in vitro, H3K4me1-marked nucleosomes are more efficiently remodeled by the BAF complex. Crystal structures of the BAF component BAF45C indicate that monomethylation, but not trimethylation, is accommodated by BAF45C's H3K4-binding site. Our results suggest that H3K4me1 has an active role at enhancers by facilitating binding of the BAF complex and possibly other chromatin regulators. PubMed: 29255264DOI: 10.1038/s41588-017-0015-6 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.2 Å) |
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