New insights into ubiquitin E3 ligase mechanism

被引：697

作者：

Berndsen, Christopher E. ^{[1
]}

Wolberger, Cynthia ^{[2
,3
]}

机构：

[1] James Madison Univ, Dept Chem & Biochem, Harrisonburg, VA 22807 USA

[2] Johns Hopkins Univ, Sch Med, Dept Biophys & Biophys Chem, Baltimore, MD 21205 USA

[3] Johns Hopkins Univ, Sch Med, Howard Hughes Med Inst, Baltimore, MD 21205 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2014年 / 21卷 / 04期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

CONJUGATING ENZYME E2; LINEAR POLYUBIQUITIN CHAINS; RING-RING COMPLEX; STRUCTURAL BASIS; ALLOSTERIC ACTIVATION; CRYSTAL-STRUCTURE; DOMAIN; PROTEINS; REVEALS; PARKIN;

D O I：

10.1038/nsmb.2780

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：

E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct classes of E3 ligases have been identified that stimulate transfer of ubiquitin and ubiquitin-like proteins through either a direct or an indirect mechanism. Only recently have the catalytic mechanisms of E3 ligases begun to be elucidated.

引用

页码：301 / 307

页数：7

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