Bromodomain

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.

Discovery
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.