Bromodomain
Bromodomains are a family of evolutionarily conserved protein modules of approximately 110 amino acids that have been found in chromatin-associated proteins as well as nuclear histone acetyltransferases (HATs). Besides its role in chromatin remodeling, recent studies have identified that bromodomains, as acetyl-lysine binding domains, are able to recognize and bind ε–N-acetylated lysine residues in histone and non-histone proteins. The nuclear magnetic resonance (NMR) spectroscopic analysis reveals that the chemical structure of bromodomains, consisting of four left-handed α-helices (including αZ, αA, αB and αC) connected by two loops (ZA and BC loops), forms a deep hydrophobic cavity serving as the acetyl-lysine recognition site.
- A4490 I-CBP 112Target: CREBBP|EP300Summary: CBP/EP300 bromodomain inhibitor
- A4491 SGC-CBP302 CitationTarget: CREBBP|EP300Summary: Inhibitor of CREBBP/EP300 bromodomain,potent
- A8810 UNC669Summary: L3MBTL antagonist,potent and selective
- B1499 RVX-2082 CitationSummary: Potent BET bromodomain inhibitor
- B1498 I-BET-7624 CitationTarget: BromodomainsSummary: BET inhibitor,highly potent
- B1500 I-BET151 (GSK1210151A)2 CitationTarget: Bromodomain and Extra-Terminal motif (BET)Summary: Selective BET inhibitor
- B5670 I-BET 151 hydrochloride1 CitationSummary: BET bromodomain inhibitor
- B4895 OF-1Summary: BRPF1B and BRPF2 bromodomain inhibitor
- B4915 BAZ2-ICRSummary: Selective BAZ2 bromodomain inhibitor
- B4916 GSK 5959Summary: BRPF1 bromodomain inhibitor