3C1C

The effect of H3 K79 dimethylation and H4 K20 trimethylation on nucleosome and chromatin structure

3C1C の概要

• エントリーDOI: 10.2210/pdb3c1c/pdb
• 関連するPDBエントリー: 1AOI 1f66 1KX3 1kx4 1KX5 1ZLA 3C1B
• 分子名称: Histone H3-like, Histone H4, Histone H2A type 1, ... (6 entities in total)
• 機能のキーワード: nucleosome, chromatin, histone h3, trimethylation, histone modification, nucleosomal surface, nucleosomal array, acetylation, chromosomal protein, dna-binding, methylation, nucleosome core, nucleus, phosphoprotein, ubl conjugation, structural protein-dna complex, structural protein/dna
• 由来する生物種: Xenopus laevis (clawed frog,common platanna,platanna); 詳細
• 細胞内の位置: Nucleus: P02302 P62799 P06897; Nucleus (By similarity): Q28D68
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 198902.65

構造登録者

Lu, X.,Simon, M.,Chodaparambil, J.,Hansen, J.,Shokat, K.,Luger, K. (登録日: 2008-01-22, 公開日: 2008-10-07, 最終更新日: 2024-11-13)

主引用文献

Lu, X.,Simon, M.D.,Chodaparambil, J.V.,Hansen, J.C.,Shokat, K.M.,Luger, K.
The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure.
Nat.Struct.Mol.Biol., 15:1122-1124, 2008

PubMed Abstract: Histone methylation regulates chromatin function dependent on the site and degree of the modification. In addition to creating binding sites for proteins, methylated lysine residues are likely to influence chromatin structure directly. Here we present crystal structures of nucleosomes reconstituted with methylated histones and investigate the folding behavior of resulting arrays. We demonstrate that dimethylation of histone H3 at lysine residue 79 locally alters the nucleosomal surface, whereas trimethylation of H4 at lysine residue 20 affects higher-order structure.

PubMed: 18794842
DOI: 10.1038/nsmb.1489

実験手法

X-RAY DIFFRACTION (3.15 Å)