Download MendeleyStructural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes.
Nam, Y., Sliz, P., Song, L., Aster, J.C., Blacklow, S.C.(2006) Cell 124: 973-983
- PubMed: 16530044
- DOI: https://doi.org/10.1016/j.cell.2005.12.037
- Primary Citation of Related Structures:
2F8X, 2F8Y - PubMed 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.
Organizational Affiliation:
Biological and Biomedical Sciences Graduate Program in the Division of Medical Sciences, Harvard Medical School, Boston, MA 02115, USA.
