Recent progress with FKBP-derived destabilizing domains

被引：33

作者：

Chu, Bernard W. ^{[1
]}

Banaszynski, Laura A. ^{[1
]}

Chen, Ling-chun ^{[1
]}

Wandless, Thomas J. ^{[1
]}

机构：

[1] Stanford Univ, Dept Chem & Syst Biol, Stanford, CA 94305 USA

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2008年 / 18卷 / 22期

关键词：

Protein degradation; Proteasome; Cell cycle; Cyclin; Shield-1; Destabilizing domain;

D O I：

10.1016/j.bmcl.2008.09.043

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The FKBP-derived destabilizing domains are increasingly being used to confer small molecule-dependent stability to many different proteins. The L106P domain confers instability to yellow fluorescent protein when it is fused to the N-terminus, the C-terminus, or spliced into the middle of yellow fluorescent protein, however multiple copies of L106P do not confer greater instability. These engineered destabilizing domains are not dominant to endogenous degrons that regulate protein stability. (C) 2008 Elsevier Ltd. All rights reserved.

引用

页码：5941 / 5944

页数：4

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