4YYM

Crystal structure of TAF1 BD2 Bromodomain bound to a butyryllysine peptide

4YYM の概要

• エントリーDOI: 10.2210/pdb4yym/pdb
• 関連するPDBエントリー: 4YY4 4YY6 4YYD 4YYG 4YYH 4YYI 4YYJ 4YYK 4YYN
• 分子名称: Transcription initiation factor TFIID subunit 1, Histone H4, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: bromodomain-butyryllysine complex, protein binding
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus : P21675 P62805
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 34307.57

構造登録者

Tang, Y.,Bellon, S.,Cochran, A.G.,Poy, F. (登録日: 2015-03-24, 公開日: 2015-09-16, 最終更新日: 2023-09-27)

主引用文献

Flynn, E.M.,Huang, O.W.,Poy, F.,Oppikofer, M.,Bellon, S.F.,Tang, Y.,Cochran, A.G.
A Subset of Human Bromodomains Recognizes Butyryllysine and Crotonyllysine Histone Peptide Modifications.
Structure, 23:1801-1814, 2015

PubMed Abstract: Bromodomains are epigenetic readers that are recruited to acetyllysine residues in histone tails. Recent studies have identified non-acetyl acyllysine modifications, raising the possibility that these might be read by bromodomains. Profiling the nearly complete human bromodomain family revealed that while most human bromodomains bind only the shorter acetyl and propionyl marks, the bromodomains of BRD9, CECR2, and the second bromodomain of TAF1 also recognize the longer butyryl mark. In addition, the TAF1 second bromodomain is capable of binding crotonyl marks. None of the human bromodomains tested binds succinyl marks. We characterized structurally and biochemically the binding to different acyl groups, identifying bromodomain residues and structural attributes that contribute to specificity. These studies demonstrate a surprising degree of plasticity in some human bromodomains but no single factor controlling specificity across the family. The identification of candidate butyryl- and crotonyllysine readers supports the idea that these marks could have specific physiological functions.

PubMed: 26365797
DOI: 10.1016/j.str.2015.08.004

実験手法

X-RAY DIFFRACTION (1.5 Å)