4QF3

Crystal structure of human BAZ2B PHD zinc finger in the free form

4QF3 の概要

• エントリーDOI: 10.2210/pdb4qf3/pdb
• 関連するPDBエントリー: 4QF2
• 分子名称: Bromodomain adjacent to zinc finger domain protein 2B, ZINC ION (3 entities in total)
• 機能のキーワード: bromodomain adjacent to zinc finger domain protein 2b, kiaa1476, transcriptional regulation interacting with iswi, transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus : Q9UIF8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13349.05

構造登録者

Tallant, C.,Van Molle, I.,Chirgadze, D.Y.,Ciulli, A. (登録日: 2014-05-19, 公開日: 2014-07-02, 最終更新日: 2024-04-03)

主引用文献

Tallant, C.,Valentini, E.,Fedorov, O.,Overvoorde, L.,Ferguson, F.M.,Filippakopoulos, P.,Svergun, D.I.,Knapp, S.,Ciulli, A.
Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC.
Structure, 23:80-92, 2015

PubMed Abstract: Binding of the chromatin remodeling complex NoRC to RNA complementary to the rDNA promoter mediates transcriptional repression. TIP5, the largest subunit of NoRC, is involved in recruitment to rDNA by interactions with promoter-bound TTF-I, pRNA, and acetylation of H4K16. TIP5 domains that recognize posttranslational modifications on histones are essential for recruitment of NoRC to chromatin, but how these reader modules recognize site-specific histone tails has remained elusive. Here, we report crystal structures of PHD zinc finger and bromodomains from human TIP5 and BAZ2B in free form and bound to H3 and/or H4 histones. PHD finger functions as an independent structural module in recognizing unmodified H3 histone tails, and the bromodomain prefers H3 and H4 acetylation marks followed by a key basic residue, KacXXR. Further low-resolution analyses of PHD-bromodomain modules provide molecular insights into their trans histone tail recognition, required for nucleosome recruitment and transcriptional repression of the NoRC complex.

PubMed: 25533489
DOI: 10.1016/j.str.2014.10.017

実験手法

X-RAY DIFFRACTION (1.6 Å)