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Nat Struct Mol Biol. 2019 Oct;26(10):863-869. doi: 10.1038/s41594-019-0290-2. Epub 2019 Oct 3.

Targeting non-bromodomain chromatin readers.

Author information

1
Structural Genomics Consortium, University of Toronto, Toronto, Canada. cheryl.arrowsmith@uhnresearch.ca.
2
Department of Medical Biophysics, University of Toronto, Toronto, Canada. cheryl.arrowsmith@uhnresearch.ca.
3
Princess Margaret Cancer Centre, Toronto, Canada. cheryl.arrowsmith@uhnresearch.ca.
4
Structural Genomics Consortium, University of Toronto, Toronto, Canada.
5
Department of Pharmacology and Toxicology, University of Toronto, Toronto, Canada.

Abstract

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.

PMID:
31582844
DOI:
10.1038/s41594-019-0290-2

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