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Lysine acetylation is an epigenetic mark that is principally recognized by bromodomains, and recently structurally diverse YEATS domains also emerged as readers of lysine acetyl/acylations. Here we present a crystallography-based strategy and the discovery of fragments binding to the ENL YEATS domain, a potential drug target. Crystal structures combined with synthetic efforts led to the identification of a submicromolar binder, providing first starting points for the development of chemical probes for this reader domain family.

Original publication

DOI

10.1021/acs.jmedchem.8b01457

Type

Journal article

Journal

J Med Chem

Publication Date

13/12/2018

Volume

61

Pages

10929 - 10934