4IOR

Crystal Structure of the first bromodomain of BRD4 in complex with DMSO

4IOR の概要

• エントリーDOI: 10.2210/pdb4ior/pdb
• 関連するPDBエントリー: 4IOO 4IOQ
• 分子名称: Bromodomain-containing protein 4, 1,2-ETHANEDIOL, DIMETHYL SULFOXIDE, ... (4 entities in total)
• 機能のキーワード: bromodomain, low mw fragment, dna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: O60885
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15425.78

構造登録者

Lolli, G.,Battistutta, R. (登録日: 2013-01-08, 公開日: 2013-10-02, 最終更新日: 2024-02-28)

主引用文献

Lolli, G.,Battistutta, R.
Different orientations of low-molecular-weight fragments in the binding pocket of a BRD4 bromodomain.
Acta Crystallogr.,Sect.D, 69:2161-2164, 2013

PubMed Abstract: Bromodomains are involved in the regulation of chromatin architecture and transcription through the recognition of acetylated lysines in histones and other proteins. Many of them are considered to be relevant pharmacological targets for different pathologies. Three crystallographic structures of the N-terminal bromodomain of BRD4 in complex with low-molecular-weight fragments are presented. They show that similar molecules mimicking acetylated lysine bind the bromodomain with different orientations and exploit different interactions. It is also advised to avoid DMSO when searching for low-affinity fragments that interact with bromodomains since DMSO binds in the acetylated lysine-recognition pocket of BRD4.

PubMed: 24100334
DOI: 10.1107/S090744491301994X

実験手法

X-RAY DIFFRACTION (1.4 Å)