Crystal structure of IRF-3 in complex with CBP

被引：108

作者：

Qin, BY

Liu, C

Srinath, H

Lam, SS

Correia, JJ

Derynck, R

Lin, K ^{[1
]}

机构：

[1] Univ Massachusetts, Sch Med, Dept Mol Pharmacol & Biochem, Worcester, MA 01605 USA

[2] Univ Calif San Francisco, Dept Cell & Tissue Biol, San Francisco, CA 94143 USA

[3] Univ Calif San Francisco, Dept Anat, Cell Biol Program, San Francisco, CA 94143 USA

[4] Univ Calif San Francisco, Program Dev Biol, San Francisco, CA 94143 USA

[5] Univ Mississippi, Med Ctr, Dept Biochem, Jackson, MS 39216 USA

来源：

STRUCTURE | 2005年 / 13卷 / 09期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/j.str.2005.06.011

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Transcriptional activation of interferon beta (IFN-beta), an antiviral cytokine, requires the assembly of IRF-3 and CBP/p300 at the promoter region of the IFN-beta gene. The crystal structure of IRF-3 in complex with CBP reveals that CBP interacts with a hydrophobic surface on IRF-3, which in latent IRF-3 is covered by its autoinhibitory elements. This structural organization suggests that virus-induced phosphoactivation of IRF-3 triggers unfolding of the autoinhibitory elements and exposes the same hydrophobic surface for CBP interaction. The structure also reveals that the interacting CBP segment can exist in drastically different conformations, depending on the identity of the associating transcription cofactor. The finding suggests a possible regulatory mechanism in CBP/p300, by which the interacting transcription factor can specify the coactivator's conformation and influence the transcriptional outcome.

引用

页码：1269 / 1277

页数：9

共 47 条

[31] Triggering the interferon antiviral response through an IKK-related pathway [J].