4L7X

Crystal structure of the DIDO PHD finger in complex with H3K4me3

4L7X の概要

• エントリーDOI: 10.2210/pdb4l7x/pdb
• 関連するPDBエントリー: 4L58
• 分子名称: Death-inducer obliterator 1, Histone H3 peptide, ZINC ION, ... (4 entities in total)
• 機能のキーワード: mitosis, chromatin, cell cycle, gene regulation
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q9BTC0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8761.73

構造登録者

Tong, Q.,Gatchalian, J.,Kutateladze, T.G. (登録日: 2013-06-14, 公開日: 2013-07-24, 最終更新日: 2025-03-26)

主引用文献

Gatchalian, J.,Futterer, A.,Rothbart, S.B.,Tong, Q.,Rincon-Arano, H.,Sanchez de Diego, A.,Groudine, M.,Strahl, B.D.,Martinez-A, C.,van Wely, K.H.,Kutateladze, T.G.
Dido3 PHD Modulates Cell Differentiation and Division.
Cell Rep, 4:148-158, 2013

PubMed Abstract: Death Inducer Obliterator 3 (Dido3) is implicated in the maintenance of stem cell genomic stability and tumorigenesis. Here, we show that Dido3 regulates the expression of stemness genes in embryonic stem cells through its plant homeodomain (PHD) finger. Binding of Dido3 PHD to histone H3K4me3 is disrupted by threonine phosphorylation that triggers Dido3 translocation from chromatin to the mitotic spindle. The crystal structure of Dido3 PHD in complex with H3K4me3 reveals an atypical aromatic-cage-like binding site that contains a histidine residue. Biochemical, structural, and mutational analyses of the binding mechanism identified the determinants of specificity and affinity and explained the inability of homologous PHF3 to bind H3K4me3. Together, our findings reveal a link between the transcriptional control in embryonic development and regulation of cell division.

PubMed: 23831028
DOI: 10.1016/j.celrep.2013.06.014

実験手法

X-RAY DIFFRACTION (1.35 Å)