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ε-N-acetylation of lysine residues (K(ac)) is one of the most abundant post-translation modifications (PTMs) in the human proteome. In the nucleus, acetylation of histones has been linked to transcriptional activation of genes but the functional consequences of most acetylation events and proteins recruited to these sites remains largely unknown. Bromodomains (BRDs) are small helical interaction modules that specifically recognize acetylation sites in proteins. BRDs have recently emerged as interesting targets for the development of specific protein interaction inhibitors, enabling a novel exiting strategy for the development of new therapies. This review provides an overview over sequence requirements of BRDs, known substrates and the structural mechanisms of specific K(ac) recognition.

Original publication

DOI

10.1016/j.febslet.2012.04.045

Type

Journal article

Journal

FEBS Lett

Publication Date

14/08/2012

Volume

586

Pages

2692 - 2704

Keywords

Acetylation, Amino Acid Motifs, Amino Acid Sequence, Binding Sites, Chromatin, DNA, Histones, Humans, Kinetics, Lysine, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Protein Interaction Mapping, Protein Structure, Secondary, Protein Structure, Tertiary, Proteins