1U35

Crystal structure of the nucleosome core particle containing the histone domain of macroH2A

1U35 の概要

• エントリーDOI: 10.2210/pdb1u35/pdb
• 関連するPDBエントリー: 1AOI 1F66
• 分子名称: alpha-satellite DNA, Histone H3.1, Hist1h4i protein, ... (6 entities in total)
• 機能のキーワード: nucleosome, ncp, histone fold, histone variant, macroh2a, structural protein-dna complex, structural protein/dna
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P68433 O75367 Q9D2U9
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 197792.12

構造登録者

Chakravarthy, S.,Gundimella, S.K.,Caron, C.,Perche, P.Y.,Pehrson, J.R.,Khochbin, S.,Luger, K. (登録日: 2004-07-20, 公開日: 2005-09-27, 最終更新日: 2023-08-23)

主引用文献

Chakravarthy, S.,Gundimella, S.K.,Caron, C.,Perche, P.Y.,Pehrson, J.R.,Khochbin, S.,Luger, K.
Structural characterization of the histone variant macroH2A.
Mol.Cell.Biol., 25:7616-7624, 2005

PubMed Abstract: macroH2A is an H2A variant with a highly unusual structural organization. It has a C-terminal domain connected to the N-terminal histone domain by a linker. Crystallographic and biochemical studies show that changes in the L1 loop in the histone fold region of macroH2A impact the structure and potentially the function of nucleosomes. The 1.6-A X-ray structure of the nonhistone region reveals an alpha/beta fold which has previously been found in a functionally diverse group of proteins. This region associates with histone deacetylases and affects the acetylation status of nucleosomes containing macroH2A. Thus, the unusual domain structure of macroH2A integrates independent functions that are instrumental in establishing a structurally and functionally unique chromatin domain.

PubMed: 16107708
DOI: 10.1128/MCB.25.17.7616-7624.2005

実験手法

X-RAY DIFFRACTION (3 Å)