Compact Parkin only: insights into the structure of an autoinhibited ubiquitin ligase

被引：15

作者：

Byrd, R. Andrew ^{[1
]}

Weissman, Allan M. ^{[2
]}

机构：

[1] Natl Canc Inst, Ctr Canc Res, Struct Biophys Lab, Frederick, MD USA

[2] Natl Canc Inst, Ctr Canc Res, Lab Prot Dynam & Signaling, Frederick, MD USA

来源：

EMBO JOURNAL | 2013年 / 32卷 / 15期

关键词：

MECHANISMS; DOMAIN; HHARI; E3;

D O I：

10.1038/emboj.2013.158

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Mutations in Parkin represent similar to 50% of disease-causing defects in autosomal recessive-juvenile onset Parkinson's disease (AR-JP). Recently, there have been four structural reports of autoinhibited forms of this RING-IBR-RING (RBR) ubiquitin ligase (E3) by the Gehring, Komander, Johnston and Shaw groups. The important advances from these studies set the stage for the next steps in understanding the molecular basis for Parkinson's disease (PD).

引用

页码：2087 / 2089

页数：3

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