The Notch transcription activation complex makes its move.

Cell ·Vol. 124 ·No. 5 ·2006-03-10 ·Pages 883-5

Barrick D, Kopan R

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.

MeSH Terms

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

Chemicals

Macromolecular Substances Receptors, Notch

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Barrick Doug

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

Kopan Raphael

Article Info

Journal

Cell

Abbr.

Cell

ISSN

0092-8674

DOI

10.1016/j.cell.2006.02.028

Published

2006-03-10

Pages

883-5

Language

English

Region

United States

NLM ID

0413066

Subset

Corrections

CommentOn

PMID: 16530044

CommentOn

PMID: 16530045

External Links

PubMed source DOI: 10.1016/j.cell.2006.02.028 View journal details

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The Notch transcription activation complex makes its move.

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