Structural basis of ubiquitylation

被引：55

作者：

VanDemark, AP ^{[1
]}

Hill, CP ^{[1
]}

机构：

[1] Univ Utah, Dept Biochem, Salt Lake City, UT 84132 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2002年 / 12卷 / 06期

关键词：

D O I：

10.1016/S0959-440X(02)00389-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The attachment of the small protein ubiquitin to other proteins, a process known as ubiquitylation, is a widespread form of post-translational modification that regulates numerous cellular functions in eukaryotes. Ubiquitylation is performed by complexes of E2 and E3 enzymes that are assembled and select substrates via a series of protein-protein interactions. Recent structure determinations of the ubiquitylation machinery have revealed some of the various protein-protein interfaces involved.

引用

页码：822 / 830

页数：9

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