The Notch transcription activation complex makes its move.
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.
Barrick
Doug
D
T.C. Jenkins Department of Biophysics, The Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
Kopan
Raphael
R
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
D046911:Macromolecular Substances; D051880:Receptors, Notch