8YXW

TRIP4 ASCH domain in complex with a 12bp dsDNA (5'-TGAGGTACCTCC-3')

8YXW の概要

• エントリーDOI: 10.2210/pdb8yxw/pdb
• 分子名称: Activating signal cointegrator 1, DNA (5'-D(*GP*GP*AP*GP*GP*TP*AP*CP*CP*TP*CP*A)-3'), DNA (5'-D(*TP*GP*AP*GP*GP*TP*AP*CP*CP*TP*CP*C)-3'), ... (4 entities in total)
• 機能のキーワード: asch domain, complex, dna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 39831.52

構造登録者

Ding, J.,Yang, H.,Hu, C. (登録日: 2024-04-03, 公開日: 2024-06-26, 最終更新日: 2024-08-28)

主引用文献

Hu, C.,Chen, Z.,Wang, G.,Yang, H.,Ding, J.
Biochemical and structural characterization of the DNA-binding properties of human TRIP4 ASCH domain reveals insights into its functional role.
Structure, 32:1208-, 2024

PubMed Abstract: TRIP4 is a conserved transcriptional coactivator that is involved in the regulation of the expression of multiple genes. It consists of a classical N-terminal C2HC5-like zinc-finger domain and a conserved C-terminal ASCH domain. Here, we characterized the DNA-binding properties of the human TRIP4 ASCH domain. Our biochemical data show that TRIP4-ASCH has comparable binding affinities toward ssDNA and dsDNA of different lengths, sequences, and structures. The crystal structures reveal that TRIP4-ASCH binds to DNA substrates in a sequence-independent manner through two adjacent positively charged surface patches: one binds to the 5'-end of DNA, and the other binds to the 3'-end of DNA. Further mutagenesis experiments and binding assays confirm the functional roles of key residues involved in DNA binding. In summary, our data demonstrate that TRIP4-ASCH binds to the 5' and 3'-ends of DNA in a sequence-independent manner, which will facilitate further studies of the biological function of TRIP4.

PubMed: 38870938
DOI: 10.1016/j.str.2024.05.012

実験手法

X-RAY DIFFRACTION (2.1 Å)