Format

Send to

Choose Destination
Mol Cell. 2001 Sep;8(3):581-90.

A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies.

Author information

1
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.

Abstract

The transcriptional coactivators CBP and p300 are critical regulators of metazoan gene expression. They associate with many different DNA-bound transcription factors through small, conserved domains. We have identified a compactly folded 46 residue domain in CBP and p300, the IRF-3 binding domain (IBiD), and we have determined its structure by NMR. It has a helical framework containing an apparently flexible polyglutamine loop that participates in ligand binding. Spectroscopic data indicate that induced folding accompanies association of IBiD with its partners, which exhibit no evident sequence similarities. We demonstrate the significance both in vitro and in vivo of interactions between IBiD and a number of diverse partners. Thus, IBiD is an important contributor to signal integration by CBP and p300.

PMID:
11583620
DOI:
10.1016/s1097-2765(01)00333-1
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center