Structural insights into the degradation of Mcl-1 induced by BH3 domains

被引：385

作者：

Czabotar, Peter E.

Lee, Erinna F.

van Delft, Mark F.

Day, Catherine L.

Smith, Brian J.

Huang, David C. S.

Fairlie, W. Douglas

Hinds, Mark G.

Colman, Peter M. ^{[1
]}

机构：

[1] Walter & Eliza Hall Inst Med Res, Parkville, Vic 3050, Australia

[2] Univ Melbourne, Dept Med Biol, Parkville, Vic 3050, Australia

[3] Univ Otago, Dept Biochem, Dunedin 9001, New Zealand

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2007年 / 104卷 / 15期

基金：

英国惠康基金;

关键词：

apoptosis; Bim; Noxa; crystallography;

D O I：

10.1073/pnas.0701297104

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Apoptosis is held in check by prosurvival proteins of the Bcl-2 family. The distantly related BH3-only proteins bind to and antagonize them, thereby promoting apoptosis. Whereas binding of the BH3-only protein Noxa to prosurvival Mcl-1 induces Mcl-1 degradation by the proteasome, binding of another BH3-only ligand, Bim, elevates Mcl-1 protein levels. We compared the three-dimensional structures of the complexes formed between BH3 peptides of both Bim and Noxa, and we show that a discrete C-terminal sequence of the Noxa BH3 is necessary to instigate Mcl-1 degradation.

引用

页码：6217 / 6222

页数：6

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