4HGA

Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX

4HGA の概要

• エントリーDOI: 10.2210/pdb4hga/pdb
• 分子名称: Death domain-associated protein 6, Histone H3.3, Histone H4, ... (5 entities in total)
• 機能のキーワード: histone chaperone, chaperone-apoptosis complex, chaperone/apoptosis
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: Q9UER7; Nucleus: P84243 P62805
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 52908.33

構造登録者

Liu, C.P.,Xiong, C.Y.,Wang, M.Z.,Yu, Z.L.,Yang, N.,Chen, P.,Zhang, Z.G.,Li, G.H.,Xu, R.M. (登録日: 2012-10-07, 公開日: 2012-11-07, 最終更新日: 2024-03-20)

主引用文献

Liu, C.P.,Xiong, C.Y.,Wang, M.Z.,Yu, Z.L.,Yang, N.,Chen, P.,Zhang, Z.G.,Li, G.H.,Xu, R.M.
Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX.
Nat.Struct.Mol.Biol., 19:1287-1292, 2012

PubMed Abstract: Mammalian histone H3.3 is a variant of the canonical H3.1 essential for genome reprogramming in fertilized eggs and maintenance of chromatin structure in neuronal cells. An H3.3-specific histone chaperone, DAXX, directs the deposition of H3.3 onto pericentric and telomeric heterochromatin. H3.3 differs from H3.1 by only five amino acids, yet DAXX can distinguish the two with high precision. By a combination of structural, biochemical and cell-based targeting analyses, we show that Ala87 and Gly90 are the principal determinants of human H3.3 specificity. DAXX uses a shallow hydrophobic pocket to accommodate the small hydrophobic Ala87 of H3.3, whereas a polar binding environment in DAXX prefers Gly90 in H3.3 over the hydrophobic Met90 in H3.1. An H3.3-H4 heterodimer is bound by the histone-binding domain of DAXX, which makes extensive contacts with both H3.3 and H4.

PubMed: 23142979
DOI: 10.1038/nsmb.2439

実験手法

X-RAY DIFFRACTION (2.799 Å)