1TTU: Crystal Structure Of Csl Bound To Dna

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.
PDB ID: 1TTUDownload
MMDB ID: 103945
PDB Deposition Date: 2004/6/23
Updated in MMDB: 2012/10
Experimental Method:
x-ray diffraction
Resolution: 2.85  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 1TTU: trimeric; determined by author
Molecular Components in 1TTU
Label Count Molecule
Protein (1 molecule)
Lin-12 and Glp-1 Transcriptional Regulator
Molecule annotation
Nucleotides(2 molecules)
5'- D(*tp*tp*ap*cp*tp*gp*tp*gp*gp*gp*ap*ap*ap*gp*a)-3'
Molecule annotation
5'- D(*ap*ap*tp*cp*tp*tp*tp*cp*cp*cp*ap*cp*ap*gp*t)-3'
Molecule annotation
Chemicals (9 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB