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Bromodomains are epigenetic reader domains that have recently become popular targets. In contrast to BET bromodomains, which have proven druggable, bromodomains from other regions of the phylogenetic tree have shallower pockets. We describe successful targeting of the challenging BAZ2B bromodomain using biophysical fragment screening and structure-based optimization of high ligand-efficiency fragments into a novel series of low-micromolar inhibitors. Our results provide attractive leads for development of BAZ2B chemical probes and indicate the whole family may be tractable.

More information Original publication

DOI

10.1021/jm401582c

Type

Journal article

Publication Date

2013-12-27T00:00:00+00:00

Volume

56

Pages

10183 - 10187

Total pages

4

Keywords

Drug Design, Humans, Ligands, Models, Molecular, Molecular Structure, Proteins, Structure-Activity Relationship, Transcription Factors, General, Zinc Fingers, Bromodomain Containing Proteins