1ZR5

Crystal structure of the macro-domain of human core histone variant macroH2A1.2

1ZR5 の概要

• エントリーDOI: 10.2210/pdb1zr5/pdb
• 関連するPDBエントリー: 1ZQ0 1ZR3
• 分子名称: H2AFY protein (2 entities in total)
• 機能のキーワード: chromatin, histone, a1pp, macro-domain, p-loop, splicing, gene regulation
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: O75367
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45413.73

構造登録者

Kustatscher, G.,Hothorn, M.,Pugieux, C.,Scheffzek, K.,Ladurner, A.G. (登録日: 2005-05-19, 公開日: 2005-06-21, 最終更新日: 2023-08-23)

主引用文献

Kustatscher, G.,Hothorn, M.,Pugieux, C.,Scheffzek, K.,Ladurner, A.G.
Splicing regulates NAD metabolite binding to histone macroH2A.
Nat.Struct.Mol.Biol., 12:624-625, 2005

PubMed Abstract: Histone macroH2A is a hallmark of mammalian heterochromatin. Here we show that human macroH2A1.1 binds the SirT1-metabolite O-acetyl-ADP-ribose (OAADPR) through its macro domain. The 1.6-A crystal structure and mutants reveal how the metabolite is recognized. Mutually exclusive exon use in the gene H2AFY produces macroH2A1.2, whose tissue distribution differs. MacroH2A1.2 shows only subtle structural changes but cannot bind nucleotides. Alternative splicing may thus regulate the binding of nicotinamide adenine dinucleotide (NAD) metabolites to chromatin.

PubMed: 15965484
DOI: 10.1038/nsmb956

実験手法

X-RAY DIFFRACTION (2.92 Å)