3TX7
Crystal structure of LRH-1/beta-catenin complex
3TX7 の概要
| エントリーDOI | 10.2210/pdb3tx7/pdb |
| 分子名称 | Catenin beta-1, Nuclear receptor subfamily 5 group A member 2, (2S)-3-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-2-[(6E)-HEXADEC-6-ENOYLOXY]PROPYL (8E)-OCTADEC-8-ENOATE (3 entities in total) |
| 機能のキーワード | lrh-1, beta-catenin, armadillo repeat, nuclear receptor ligand binding domain, protein binding |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Cytoplasm: P35222 Nucleus (Probable): O00482 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 98272.31 |
| 構造登録者 | |
| 主引用文献 | Yumoto, F.,Nguyen, P.,Sablin, E.P.,Baxter, J.D.,Webb, P.,Fletterick, R.J. Structural basis of coactivation of liver receptor homolog-1 by beta-catenin. Proc.Natl.Acad.Sci.USA, 109:143-148, 2012 Cited by PubMed Abstract: We report the three-dimensional structure of a β-catenin armadillo repeat in complex with the liver receptor homolog-1 (LRH-1) ligand binding domain at 2.8 Å resolution as the first structure of β-catenin in complex with any nuclear receptor. The surface of β-catenin that binds LRH-1 partly overlaps defined contact sites for peptide segments of β-catenin partners, including T-cell factor-4. The surface of LRH-1 that engages β-catenin is comprised of helices 1, 9, and 10 and is distinct from known interaction surfaces of LRH-1, including corepressor and coactivator binding sites. Targeted mutagenesis of amino acids forming both sides of the LRH-1/β-catenin interface reveals that they are essential for stable interactions between these proteins in solution. The LRH-1 binding site in β-catenin is also required for association with androgen receptor, providing evidence that the observed LRH-1/β-catenin interaction may be prototypic. PubMed: 22187462DOI: 10.1073/pnas.1117036108 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.76 Å) |
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