Targeting non-bromodomain chromatin readers

被引：44

作者：

Arrowsmith, Cheryl H. ^{[1
,2
,3
]}

Schapira, Matthieu ^{[1
,4
]}

机构：

[1] Univ Toronto, Struct Genom Consortium, Toronto, ON, Canada

[2] Univ Toronto, Dept Med Biophys, Toronto, ON, Canada

[3] Princess Margaret Canc Ctr, Toronto, ON, Canada

[4] Univ Toronto, Dept Pharmacol & Toxicol, Toronto, ON, Canada

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2019年 / 26卷 / 10期

关键词：

METHYL-LYSINE BINDING; SMALL-MOLECULE INHIBITORS; LEUKEMIA MLL PROTEIN; HISTONE H3; STRUCTURAL BASIS; CHEMICAL PROBE; RECOGNITION; COMPLEX; ARGININE; DOMAIN;

D O I：

10.1038/s41594-019-0290-2

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：

Chromatin regulatory proteins are increasingly recognized as potential new drug targets. Many of these proteins harbor one or more so called 'reader domains' that recognize covalent modifications of lysine and arginine residues, typically on histones, which mediate specific interactions within chromatin. Here we review recent progress in the discovery of drug-like small molecules that antagonize the function of methyl-lysine and methyl-arginine reader domains (Royal family, plant homeodomain (PHD) and WD40 domains) as well as the acyl-lysine-binding YEATS domain.

引用

页码：863 / 869

页数：7

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