3OUX
Structure of beta-catenin with phosphorylated Lef-1
3OUX の概要
| エントリーDOI | 10.2210/pdb3oux/pdb |
| 関連するPDBエントリー | 3OUW |
| 分子名称 | Catenin beta-1, Lymphoid enhancer-binding factor 1 (3 entities in total) |
| 機能のキーワード | wnt/beta-catenin signaling pathway, tcf, lef, transcription factors, phosphorylation, protein binding |
| 由来する生物種 | Mus musculus (mouse) 詳細 |
| 細胞内の位置 | Cytoplasm: Q02248 Nucleus: P27782 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 66008.95 |
| 構造登録者 | |
| 主引用文献 | Sun, J.,Weis, W.I. Biochemical and structural characterization of beta-catenin interactions with nonphosphorylated and CK2-phosphorylated Lef-1. J.Mol.Biol., 405:519-530, 2011 Cited by PubMed Abstract: In the Wnt/β-catenin signaling pathway, β-catenin activates target genes through its interactions with the T-cell factor/lymphoid enhancer-binding factor (TCF/Lef) family of transcription factors. The crystal structures of complexes between the β-catenin armadillo domain and the Lef-1 N-terminal domain show that the overall conformation and many of the interactions are similar to other published structures of TCFs bound to β-catenin. However, a second salt bridge in other TCF-β-catenin structures is absent in the structure of β-catenin-Lef-1 complex, indicating that this feature is not obligatory for β-catenin binding. Casein kinase II (CK2) has been shown to act as a positive regulator of Wnt signaling, and Lef-1 is a substrate of CK2. In vitro phosphorylation of purified Lef-1 was used to examine the effect of CK2 on the interaction of Lef-1 with β-catenin. Mass spectrometry data show that CK2 phosphorylation of Lef-1 N-terminal domain results in a single phosphorylation site at Ser40. Isothermal titration calorimetry revealed that β-catenin binds to nonphosphorylated or CK2-phosphorylated Lef-1 with the same affinity, which is consistent with the absence of phospho-Ser40 interactions in the crystal structure of phosphorylated Lef-1 N-terminal domain bound to β-catenin. These data indicate that the effect of CK2 on the Wnt/β-catenin pathway does not appear to be at the level of the Lef-1-β-catenin interaction. PubMed: 21075118DOI: 10.1016/j.jmb.2010.11.010 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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