Sulindac Inhibits Canonical Wnt Signaling by Blocking the PDZ Domain of the Protein Dishevelled

被引：74
|
作者：
Lee, Ho-Jin [2 ]
Wang, Nick X. [2 ]
Shi, De-Li [1 ]
Zheng, Jie J. [2 ]
机构：
[1] Univ Paris 06, Dev Biol Lab, F-75005 Paris, France
[2] St Jude Childrens Res Hosp, Dept Biol Struct, Memphis, TN 38105 USA
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2009年 / 48卷 / 35期
关键词：
antitumor agents; hydrogen bonds; signal inhibition; signal transduction; NONSTEROIDAL ANTIINFLAMMATORY DRUGS; BETA-CATENIN; COLORECTAL-CANCER; EPIGENETIC INACTIVATION; HUMAN COUNTERPART; UP-REGULATION; NMR; TARGET; SULFONE; PATHWAY;
D O I：
10.1002/anie.200902981
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
A new application: The nonsteroidal anti-inflammatory drug sulindac interacts directly and specifically with the PDZ domain of the protein Dishevelled (Dvl), which is a key intracellular component of the Wnt signaling pathways. Sulindac binds to the conventional peptide-binding pocket of the domain (see picture), and may exert a cancer chemoprotective effect by blocking it, thereby inhibiting canonical Wnt signaling. © 2009 Wiley-VCH Verlag GmbH & Co. KCaA.
引用
收藏
页码：6448 / 6452
页数：5
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