Structural Basis for Cooperativity in Recruitment of MAML Coactivators to Notch Transcription Complexes
Copyright policy )Structural Basis for Cooperativity in Recruitment of MAML Coactivators to Notch Transcription Complexes
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.
- Harvard University United States
- Brigham and Women's Faulkner Hospital United States
- Howard Hughes Medical Institute United States
Models, Molecular, Transcriptional Activation, Transcription, Genetic, Biochemistry, Genetics and Molecular Biology(all), Macromolecular Substances, Molecular Sequence Data, Nuclear Proteins, Crystallography, X-Ray, DNA-Binding Proteins, Gene Expression Regulation, Immunoglobulin J Recombination Signal Sequence-Binding Protein, Trans-Activators, Animals, Humans, Nucleic Acid Conformation, Amino Acid Sequence, Receptor, Notch1, Promoter Regions, Genetic, Protein Structure, Quaternary, Sequence Alignment, Transcription Factors
Models, Molecular, Transcriptional Activation, Transcription, Genetic, Biochemistry, Genetics and Molecular Biology(all), Macromolecular Substances, Molecular Sequence Data, Nuclear Proteins, Crystallography, X-Ray, DNA-Binding Proteins, Gene Expression Regulation, Immunoglobulin J Recombination Signal Sequence-Binding Protein, Trans-Activators, Animals, Humans, Nucleic Acid Conformation, Amino Acid Sequence, Receptor, Notch1, Promoter Regions, Genetic, Protein Structure, Quaternary, Sequence Alignment, Transcription Factors
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