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Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes



Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes



Cell 124(5): 973-983



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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Accession: 012588089

Download citation: RISBibTeXText

PMID: 16530044

DOI: 10.1016/j.cell.2005.12.037


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