3TUO

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

Summary for 3TUO

• Entry DOI: 10.2210/pdb3tuo/pdb
• Descriptor: DNA-binding protein SATB1 (2 entities in total)
• Functional Keywords: dna binding, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus matrix: Q01826
• Total number of polymer chains: 4
• Total formula weight: 46633.38

Authors

Wang, Z.,Yang, X.,Long, J.,Shen, Y. (deposition date: 2011-09-17, release date: 2012-02-01, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.697 Å)