The Notch transcription activation complex makes its move

Doug Barrick; Raphael Kopan

doi:10.1016/j.cell.2006.02.028

The Notch transcription activation complex makes its move

Cell. 2006 Mar 10;124(5):883-5. doi: 10.1016/j.cell.2006.02.028.

Authors

Doug Barrick¹, Raphael Kopan

Affiliation

¹ T.C. Jenkins Department of Biophysics, The Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.

PMID: 16530033
DOI: 10.1016/j.cell.2006.02.028

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.

Publication types

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MeSH terms

Allosteric Regulation
Animals
Humans
Macromolecular Substances
Models, Molecular
Protein Binding
Protein Conformation*
Receptors, Notch* / chemistry
Receptors, Notch* / metabolism
Transcription, Genetic*
Transcriptional Activation*

Substances

Macromolecular Substances
Receptors, Notch