A structure-based approach towards identification of inhibitory fragments for eleven-nineteen-leukemia protein (ENL) YEATS domain

BioRxiv : the Preprint Server for Biology
David HeidenreichStefan Knapp

Abstract

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 sub-micromolar binder, providing first starting points for the development of chemical probes for this reader domain family.

Related Concepts

Acetylation
Crystallography
Lysine
Cytochrome-c Oxidase Deficiency
Crystal Structure
Structure
Bromodomain Containing Protein 2
ELL protein, human
Epigenetic Process
Transcriptional Activation Domain

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