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.
- A4184 PFI-1 (PF-6405761)1 CitationTarget: BromodomainsSummary: BET inhibitor
- A4186 Bromosporine1 CitationTarget: BromodomainsSummary: Bromodomain inhibitor,non-selective
- A1910 Bromodomain Inhibitor, (+)-JQ138 CitationTarget: BromodomainsSummary: BET bromodomain inhibitor
- A3445 GSK 525768ASummary: inactive stereoisomer of I-BET-762
- A3692 OTX-0153 CitationTarget: BromodomainsSummary: BRD inhibitor
- A3901 UNC12151 CitationTarget: L3MBTLSummary: Chemical probe for the methyllysine (Kme)
- 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