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

Citation
Ch. Lin et al., A small domain of CBP/p300 binds diverse proteins: Solution structure and functional studies, MOL CELL, 8(3), 2001, pp. 581-590
Citations number
59
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Cell & Developmental Biology
Journal title
MOLECULAR CELL
ISSN journal
1097-2765 → ACNP
Volume
8
Issue
3
Year of publication
2001
Pages
581 - 590
Database
ISI
SICI code
1097-2765(200109)8:3<581:ASDOCB>2.0.ZU;2-1
Abstract
The transcriptional coactivators CBP and p300 are critical regulators of me tazoan gene expression. They associate with many different DNA-bound transc ription factors through small, conserved domains. We have identified a comp actly folded 46 residue domain in CBP and p300, the IRF-3 binding domain (I BiD), and we have determined its structure by NMR. It has a helical framewo rk containing an apparently flexible polyglutamine loop that participates i n ligand binding. Spectroscopic data indicate that induced folding accompan ies association of IBiD with its partners, which exhibit no evident sequenc e similarities. We demonstrate the significance both in vitro and in vivo o f interactions between IBiD and a number of diverse partners. Thus, IBiD is an important contributor to signal integration by CBP and p300.