Structure of SET domain proteins: a new twist on histone methylation

被引：90

作者：

Marmorstein, R ^{[1
]}

机构：

[1] Univ Penn, Dept Chem, Wistar Inst, Philadelphia, PA 19104 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2003年 / 28卷 / 02期

关键词：

D O I：

10.1016/S0968-0004(03)00007-0

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 methylation of lysine residues on histone tails is catalyzed by proteins containing a conserved SET domain. A recent flurry of structures of SET domain proteins has revealed a new protein fold and a scaffold for understanding catalysis and substrate binding by these enzymes. The prospect that histone methylation might form an epigenetic code and the implicated involvement of SET domain proteins in cancer assures that structure-function studies of these enzymes will continue until their detailed mechanism of action is determined.

引用

页码：59 / 62

页数：4

共 18 条

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