5I3L

DPF3b in complex with H3K14ac peptide

5I3L の概要

• エントリーDOI: 10.2210/pdb5i3l/pdb
• 分子名称: Zinc finger protein DPF3, H3K14ac peptide, ZINC ION, ... (7 entities in total)
• 機能のキーワード: structural genomics, structural genomics consortium, sgc, peptide binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 28601.26

構造登録者

Tempel, W.,Liu, Y.,Walker, J.R.,Zhao, A.,Qin, S.,Loppnau, P.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (登録日: 2016-02-10, 公開日: 2016-02-24, 最終更新日: 2024-11-13)

主引用文献

Li, W.,Zhao, A.,Tempel, W.,Loppnau, P.,Liu, Y.
Crystal structure of DPF3b in complex with an acetylated histone peptide.
J.Struct.Biol., 195:365-372, 2016

PubMed Abstract: Histone acetylation plays an important role in chromatin dynamics and is associated with active gene transcription. This modification is written by acetyltransferases, erased by histone deacetylases and read out by bromodomain containing proteins, and others such as tandem PHD fingers of DPF3b. Here we report the high resolution crystal structure of the tandem PHD fingers of DPF3b in complex with an H3K14ac peptide. In the complex structure, the histone peptide adopts an α-helical conformation, unlike previously observed by NMR, but similar to a previously reported MOZ-H3K14ac complex structure. Our crystal structure adds to existing evidence that points to the α-helix as a natural conformation of histone tails as they interact with histone-associated proteins.

PubMed: 27402533
DOI: 10.1016/j.jsb.2016.07.001

実験手法

X-RAY DIFFRACTION (1.85 Å)