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The bromodomain: From epigenome reader to druggable target.

Authors: Sanchez, R  Meslamani, J  Zhou, MM 
Citation: Sanchez R, etal., Biochim Biophys Acta. 2014 Aug;1839(8):676-685. doi: 10.1016/j.bbagrm.2014.03.011. Epub 2014 Mar 28.
Pubmed: (View Article at PubMed) PMID:24686119
DOI: Full-text: DOI:10.1016/j.bbagrm.2014.03.011

Lysine acetylation is a fundamental post-translational modification that plays an important role in the control of gene transcription in chromatin in an ordered fashion. The bromodomain, the conserved structural module present in transcription-associated proteins, functions exclusively to recognize acetyl-lysine on histones and non-histone proteins. The structural analyses of bromodomains' recognition of lysine-acetylated peptides derived from histones and cellular proteins provide detailed insights into the differences and unifying features of biological ligand binding selectivity by the bromodomains. Newly developed small-molecule inhibitors targeting bromodomain proteins further highlight the functional importance of bromodomain/acetyl-lysine binding as a key mechanism in orchestrating molecular interactions and regulation in chromatin biology and gene transcription. These new studies argue that modulating bromodomain/acetyl-lysine interactions with small-molecule chemicals offer new opportunities to control gene expression in a wide array of human diseases including cancer and inflammation. This article is part of a Special Issue entitled: Molecular mechanisms of histone modification function.

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CRRD Object Information
CRRD ID: 9479075
Created: 2014-08-26
Species: All species
Last Modified: 2014-08-26
Status: ACTIVE



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