2FO1

Crystal Structure of the CSL-Notch-Mastermind ternary complex bound to DNA

2FO1 の概要

• エントリーDOI: 10.2210/pdb2fo1/pdb
• 分子名称: 5'-D(*TP*TP*AP*CP*TP*GP*TP*GP*GP*GP*AP*AP*AP*GP*A)-3', 5'-D(*AP*AP*TP*CP*TP*TP*TP*CP*CP*CP*AP*CP*AP*GP*T)-3', Lin-12 and glp-1 phenotype protein 1, isoform b, ... (5 entities in total)
• 機能のキーワード: beta-barrel, protein-dna complex, double helix, ankyrin repeat, gene regulation-signalling protein-dna complex, gene regulation/signalling protein/dna
• 由来する生物種: Caenorhabditis elegans; 詳細
• 細胞内の位置: Nucleus: Q09260; Membrane; Single-pass type I membrane protein: P14585
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 115151.65

構造登録者

Wilson, J.J.,Kovall, R.A. (登録日: 2006-01-12, 公開日: 2006-03-21, 最終更新日: 2024-11-20)

主引用文献

Wilson, J.J.,Kovall, R.A.
Crystal structure of the CSL-Notch-Mastermind ternary complex bound to DNA.
Cell(Cambridge,Mass.), 124:985-996, 2006

PubMed Abstract: Notch signaling mediates communication between cells and is essential for proper embryonic patterning and development. CSL is a DNA binding transcription factor that regulates transcription of Notch target genes by interacting with coregulators. Transcriptional activation requires the displacement of corepressors from CSL by the intracellular portion of the receptor Notch (NotchIC) and the recruitment of the coactivator protein Mastermind to the complex. Here we report the 3.1 A structure of the ternary complex formed by CSL, NotchIC, and Mastermind bound to DNA. As expected, the RAM domain of Notch interacts with the beta trefoil domain of CSL; however, the C-terminal domain of CSL has an unanticipated central role in the interface formed with the Notch ankyrin repeats and Mastermind. Ternary complex formation induces a substantial conformational change within CSL, suggesting a molecular mechanism for the conversion of CSL from a repressor to an activator.

PubMed: 16530045
DOI: 10.1016/j.cell.2006.01.035

実験手法

X-RAY DIFFRACTION (3.12 Å)