title: The Notch transcription activation complex makes its move.
abstract: Two papers in this issue of Cell, (Nam et al., 2006; Wilson and Kovall, 2006) report the crystal structure of the Notch transcriptional activation complex. These structures show that the ANK domain of Notch is an integral part of the transcription complex and supports MAM binding, whereas the RAM domain may trigger allosteric changes in the structure needed for the derepression of transcription.
authors.affiliation: T.C. Jenkins Department of Biophysics, The Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
authors.forename: Doug
authors.initials: D
authors.lastname: Barrick
authors.forename: Raphael
authors.initials: R
authors.lastname: Kopan
mesh_terms: D000494:Allosteric Regulation; D000818:Animals; D006801:Humans; D046911:Macromolecular Substances; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D051880:Receptors, Notch / Q000737:chemistry / Q000378:metabolism; D014158:Transcription, Genetic; D015533:Transcriptional Activation
chemical_list: D046911:Macromolecular Substances; D051880:Receptors, Notch