8HBM

Structural basis of the farnesoid X receptor/retinoid X receptor heterodimer on inverted repeat DNA

8HBM の概要

• エントリーDOI: 10.2210/pdb8hbm/pdb
• 分子名称: Retinoic acid receptor RXR-alpha, Bile acid receptor, DNA (5'-D(P*CP*CP*GP*AP*GP*GP*TP*CP*AP*AP*TP*GP*AP*CP*CP*TP*CP*G)-3'), ... (5 entities in total)
• 機能のキーワード: fxr, rxr, dna, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 68872.15

構造登録者

Jiang, L.,Chen, Y. (登録日: 2022-10-29, 公開日: 2023-06-14, 最終更新日: 2024-05-01)

主引用文献

Jiang, L.,Liu, X.,Liang, X.,Dai, S.,Wei, H.,Guo, M.,Chen, Z.,Xiao, D.,Chen, Y.
Structural basis of the farnesoid X receptor/retinoid X receptor heterodimer on inverted repeat DNA.
Comput Struct Biotechnol J, 21:3149-3157, 2023

PubMed Abstract: Farnesoid X receptor (FXR) is a ligand-activated transcription factor known as bile acid receptor (BAR). FXR plays critical roles in various biological processes, including metabolism, immune inflammation, liver regeneration and liver carcinogenesis. FXR forms a heterodimer with the retinoid X receptor (RXR) and binds to diverse FXR response elements (FXREs) to exert its various biological functions. However, the mechanism by which the FXR/RXR heterodimer binds the DNA elements remains unclear. In this study, we aimed to use structural, biochemical and bioinformatics analyses to study the mechanism of FXR binding to the typical FXRE, such as the IR1 site, and the heterodimer interactions in the FXR-DBD/RXR-DBD complex. Further biochemical assays showed that RAR, THR and NR4A2 do not form heterodimers with RXR when bound to the IR1 sites, which indicates that IR1 may be a unique binding site for the FXR/RXR heterodimer. Our studies may provide a further understanding of the dimerization specificity of nuclear receptors.

PubMed: 37287811
DOI: 10.1016/j.csbj.2023.05.026

実験手法

X-RAY DIFFRACTION (3.3 Å)