3TUO

Crystal structure of N-terminal domain of DNA-binding protein satb1

3TUO の概要

• エントリーDOI: 10.2210/pdb3tuo/pdb
• 分子名称: DNA-binding protein SATB1 (2 entities in total)
• 機能のキーワード: dna binding, dna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus matrix: Q01826
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 46633.38

構造登録者

Wang, Z.,Yang, X.,Long, J.,Shen, Y. (登録日: 2011-09-17, 公開日: 2012-02-01, 最終更新日: 2024-03-20)

主引用文献

Wang, Z.,Yang, X.,Chu, X.,Zhang, J.,Zhou, H.,Shen, Y.,Long, J.
The structural basis for the oligomerization of the N-terminal domain of SATB1
Nucleic Acids Res., 40:4193-4202, 2012

PubMed Abstract: Special AT-rich sequence-binding protein 1 (SATB1) is a global chromatin organizer and gene expression regulator essential for T-cell development and breast cancer tumor growth and metastasis. The oligomerization of the N-terminal domain of SATB1 is critical for its biological function. We determined the crystal structure of the N-terminal domain of SATB1. Surprisingly, this domain resembles a ubiquitin domain instead of the previously proposed PDZ domain. Our results also reveal that SATB1 can form a tetramer through its N-terminal domain. The tetramerization of SATB1 plays an essential role in its binding to highly specialized DNA sequences. Furthermore, isothermal titration calorimetry results indicate that the SATB1 tetramer can bind simultaneously to two DNA targets. Based on these results, we propose a molecular model whereby SATB1 regulates the expression of multiple genes both locally and at a distance.

PubMed: 22241778
DOI: 10.1093/nar/gkr1284

実験手法

X-RAY DIFFRACTION (1.697 Å)