Structural features and inhibitors of bromodomains

Jamel Meslamani, Steven G. Smith, Roberto Sanchez, Ming Ming Zhou

Research output: Contribution to journalReview articlepeer-review

18 Scopus citations


Bromodomains are conserved structural modules responsible for recognizing acetylated-lysine residues on histone tails and other transcription-associated proteins, such as transcription factors and co-factors. Owing to their important functions in the regulation of ordered gene transcription in chromatin, bromodomains of the BET family proteins have recently been shown as druggable targets for a wide array of human diseases, including cancer and inflammation. Here we review the structural and functional features of the bromodomains and their small-molecule inhibitors. Additional new insights provided herein highlight the landscape of the ligand binding sites in the bromodomains that will hopefully facilitate further development of new inhibitors with optimal affinity and selectivity.

Original languageEnglish
Pages (from-to)3-15
Number of pages13
JournalDrug Discovery Today: Technologies
StatePublished - 1 Mar 2016


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