Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes - PubMed (original) (raw)

. 2006 Mar 10;124(5):973-83.

doi: 10.1016/j.cell.2005.12.037.

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• PMID: 16530044
• DOI: 10.1016/j.cell.2005.12.037

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

Yunsun Nam et al. Cell. 2006.

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Abstract

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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Comment in

• The Notch transcription activation complex makes its move.
  Barrick D, Kopan R. Barrick D, et al. Cell. 2006 Mar 10;124(5):883-5. doi: 10.1016/j.cell.2006.02.028. Cell. 2006. PMID: 16530033

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