1QZ7
Beta-catenin binding domain of Axin in complex with beta-catenin
1QZ7 の概要
| エントリーDOI | 10.2210/pdb1qz7/pdb |
| 分子名称 | Beta-catenin, Axin (3 entities in total) |
| 機能のキーワード | beta-catenin, axin, protein-protein complex, cell adhesion |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Cytoplasm: P35222 Cytoplasm (By similarity): Q9YGY0 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 65968.03 |
| 構造登録者 | |
| 主引用文献 | Xing, Y.,Clements, W.K.,Kimelman, D.,Xu, W. Crystal structure of a beta-catenin/Axin complex suggests a mechanism for the {beta}-catenin destruction complex GENES DEV., 17:2753-2764, 2003 Cited by PubMed Abstract: The "beta-catenin destruction complex" is central to canonical Wnt/beta-catenin signaling. The scaffolding protein Axin and the tumor suppressor adenomatous polyposis coli protein (APC) are critical components of this complex, required for rapid beta-catenin turnover. We determined the crystal structure of a complex between beta-catenin and the beta-catenin-binding domain of Axin (Axin-CBD). The Axin-CBD forms a helix that occupies the groove formed by the third and fourth armadillo repeats of beta-catenin and thus precludes the simultaneous binding of other beta-catenin partners in this region. Our biochemical studies demonstrate that, when phosphorylated, the 20-amino acid repeat region of APC competes with Axin for binding to beta-catenin. We propose that a key function of APC in the beta-catenin destruction complex is to remove phosphorylated beta-catenin product from the active site. PubMed: 14600025DOI: 10.1101/gad.1142603 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






