2F8X
Crystal structure of activated Notch, CSL and MAML on HES-1 promoter DNA sequence
Summary for 2F8X
Entry DOI | 10.2210/pdb2f8x/pdb |
Descriptor | 5'-D(*GP*TP*TP*AP*CP*TP*GP*TP*GP*GP*GP*AP*AP*AP*GP*AP*AP*A)-3', 5'-D(*TP*TP*TP*CP*TP*TP*TP*CP*CP*CP*AP*CP*AP*GP*TP*AP*AP*C)-3', Recombining binding protein suppressor of hairless, isoform 4, ... (6 entities in total) |
Functional Keywords | notch, csl, mastermind, hes-1, ankyrin repeats, rel-homology region, transcription-dna complex, transcription/dna |
Biological source | Homo sapiens (human) More |
Cellular location | Nucleus: Q06330 Cell membrane; Single-pass type I membrane protein (By similarity). Notch 1 intracellular domain: Nucleus (By similarity): P46531 Nucleus speckle: Q92585 |
Total number of polymer chains | 5 |
Total formula weight | 95742.19 |
Authors | Nam, Y.,Sliz, P.,Blacklow, S.C. (deposition date: 2005-12-04, release date: 2006-04-04, Last modification date: 2023-08-30) |
Primary citation | Nam, Y.,Sliz, P.,Song, L.,Aster, J.C.,Blacklow, S.C. Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes. Cell(Cambridge,Mass.), 124:973-983, 2006 Cited by 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. PubMed: 16530044DOI: 10.1016/j.cell.2005.12.037 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.25 Å) |
Structure validation
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