Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

A midthroughput screening follow-up program targeting the first bromodomain of the human BRD4 protein, BRD4(BD1), identified an acetylated-mimic xanthine derivative inhibitor. This compound binds with an affinity in the low micromolar range yet exerts suitable unexpected selectivity in vitro against the other members of the bromodomain and extra-terminal domain (BET) family. A structure-based program pinpointed a role of the ZA loop, paving the way for the development of potent and selective BET-BRDi probes.

Original publication

DOI

10.1021/acs.jmedchem.5b01708

Type

Journal article

Journal

J Med Chem

Publication Date

25/02/2016

Volume

59

Pages

1634 - 1641

Keywords

Acetylation, Drug Discovery, Humans, Models, Molecular, Nuclear Proteins, Protein Structure, Tertiary, Transcription Factors, Xanthines