| Bromodomain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ribbon diagram of the GCN5 bromodomain from Saccharomyces cerevisiae, colored from blue (N-terminus) to red (C-terminus).[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Bromodomain | ||||||||
| Pfam | PF00439 | ||||||||
| InterPro | IPR001487 | ||||||||
| SMART | SM00297 | ||||||||
| PROSITE | PDOC00550 | ||||||||
| SCOP | 1b91 | ||||||||
| CDD | cd04369 | ||||||||
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A bromodomain is a protein domain that recognizes acetylated lysine residues such as those on the N-terminal tails of histones. This recognition is often a prerequisite for protein-histone association and chromatin remodeling. The domain itself adopts an all-α protein fold, a bundle of four alpha helices.[1][2]
The bromodomain was identified as a novel structural motif by John W. Tamkun and colleagues studying the brm gene, and showed sequence similarity to genes involved in transcriptional activation [3].