Journal
CELL
Volume 124, Issue 5, Pages 973-983Publisher
CELL PRESS
DOI: 10.1016/j.cell.2005.12.037
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Funding
- NCI NIH HHS [R01 CA092433-03, R01 CA119130-01, CA92433, R01 CA092433-01A1, R01 CA119130, R01 CA092433-02, R01 CA092433-04, CA119130, R01 CA092433-02S1, R01 CA092433] Funding Source: Medline
- NCRR NIH HHS [P41 RR012408, P41 RR012408-108514] Funding Source: Medline
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Notch receptors transduce essential developmental signals between neighboring cells by forming a complex that leads to transcription of target genes upon activation. We report here the crystal structure of a Notch transcriptional activation complex containing the ankyrin domain of human Notch1 (ANK), the transcription factor CSL on cognate DNA, and a polypeptide from the coactivator Mastermind-like-1 (MAML-1). Together, CSL and ANK create a groove to bind the MAML-1 polypeptide as a kinked, 70 A helix. The composite binding surface likely restricts the recruitment of MAML proteins to promoters on which Notch:CSL complexes have been preassembled, ensuring tight transcriptional control of Notch target genes.
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