2IIJ

Structure of human Asf1a in complex with histone H3

2IIJ の概要

• エントリーDOI: 10.2210/pdb2iij/pdb
• 関連するPDBエントリー: 1tey
• NMR情報: BMRB: 6298
• 分子名称: ASF1A protein, Histone H3 (2 entities in total)
• 機能のキーワード: protein-protein complex, chaperone
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19931.36

構造登録者

Agez, M.,Guerois, R.,van Heijenoort, C.,Mann, C.,Ochsenbein, F. (登録日: 2006-09-28, 公開日: 2007-02-13, 最終更新日: 2024-05-29)

主引用文献

Agez, M.,Chen, J.,Guerois, R.,van Heijenoort, C.,Thuret, J.Y.,Mann, C.,Ochsenbein, F.
Structure of the histone chaperone asf1 bound to the histone h3 C-terminal helix and functional insights.
Structure, 15:191-199, 2007

PubMed Abstract: Asf1 is a histone chaperone that favors histone H3/H4 assembly and disassembly. We solved the structure of the conserved domain of human ASF1A in complex with the C-terminal helix of histone H3 using nuclear magnetic resonance spectroscopy. This structure is fully compatible with an association of ASF1 with the heterodimeric form of histones H3/H4. In our model, ASF1 substitutes for the second H3/H4 heterodimer that is normally found in heterotetrameric H3/H4 complexes. This result constitutes an essential step in the fundamental understanding of the mechanisms of nucleosome assembly by histone chaperones. Point mutations that perturb the Asf1/histone interface were designed from the structure. The decreased binding affinity of the Asf1-H3/H4 complex correlates with decreased levels of H3-K56 acetylation and phenotypic defects in vivo.

PubMed: 17292837
DOI: 10.1016/j.str.2007.01.002

実験手法

SOLUTION NMR