Bromodomain

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Ribbon diagram of the GCN5 bromodomain from Saccharomyces cerevisiae (PDB accession code 1E6I, chain A), colored from blue (N-terminus) to red (C-terminus).

A bromodomain is a protein domain that recognizes acetylated lysine residues 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.

[edit] External links

• SCOP list of bromodomains with known structures]

[edit] References

• Zeng L and Zhou MM. (2002) "Bromodomain: an acetyl-lysine binding domain", FEBS Lett., 513, 124-128.
• Owen DJ, Ornaghi P, Yang JC, Lowe N, Evans PR, Ballario P, Neuhaus D, Filetici P, Travers AA. (2000) "The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p", EMBO J., 19, 6141-6149.

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