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 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.

[edit] External links

• SCOP list of bromodomains with known structures
• PDOC00550 - Bromodomain in PROSITE

[edit] References

• Zeng L, Zhou MM (2002). "Bromodomain: an acetyl-lysine binding domain". FEBS Lett. 513 (1): 124–8. doi:10.1016/S0014-5793(01)03309-9. PMID 11911891. 
• Owen DJ, Ornaghi P, Yang JC, et al (2000). "The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p". EMBO J. 19 (22): 6141–9. doi:10.1093/emboj/19.22.6141. PMID 11080160. 

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