1TTU

Crystal Structure of CSL bound to DNA

1TTU の概要

• エントリーDOI: 10.2210/pdb1ttu/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 transcriptional regulator, ... (5 entities in total)
• 機能のキーワード: beta-trefoil domain, protein-dna complex, rel homology region, csl, notch signaling, transcription factor, transcription
• 由来する生物種: Caenorhabditis elegans; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 63497.26

構造登録者

Kovall, R.A.,Hendrickson, W.A. (登録日: 2004-06-23, 公開日: 2004-08-31, 最終更新日: 2024-02-14)

主引用文献

Kovall, R.A.,Hendrickson, W.A.
Crystal structure of the nuclear effector of Notch signaling, CSL, bound to DNA
Embo J., 23:3441-3451, 2004

PubMed Abstract: Notch signaling is a conserved pathway of communication between neighboring cells that results in cell fate specification, and CSL is the universal transcriptional effector of Notch signaling. The Notch intracellular domain translocates to the nucleus after proteolytic release upon Notch extracellular engagement, and there it displaces corepressors from DNA-bound CSL and recruits activators of Notch target genes. Here we report the 2.85 A crystal structure of CSL with a target DNA. CSL comprises three structurally integrated domains: its amino (NTD)- and carboxy (CTD)-terminal domains are strikingly similar to those of Rel transcription factors, but a surprising beta-trefoil domain (BTD) is inserted between them. CSL-bound DNA is recognized specifically by conserved residues from NTD and BTD. A hydrophobic pocket on BTD is identified as the likely site of Notch interaction with CSL, which has functional implications for the mechanism of Notch signaling.

PubMed: 15297877
DOI: 10.1038/sj.emboj.7600349

実験手法

X-RAY DIFFRACTION (2.85 Å)