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Pubmed ID :22464331
Publication Date : //

Histone recognition and large-scale structural analysis of the human bromodomain family.


Bromodomains (BRDs) are protein interaction modules that specifically recognize ε-N-lysine acetylation motifs, a key event in the reading process of epigenetic marks. The 61 BRDs in the human genome cluster into eight families based on structure/sequence similarity. Here, we present 29 high-resolution crystal structures, covering all BRD families. Comprehensive crossfamily structural analysis identifies conserved and family-specific structural features that are necessary for specific acetylation-dependent substrate recognition. Screening of more than 30 representative BRDs against systematic histone-peptide arrays identifies new BRD substrates and reveals a strong influence of flanking posttranslational modifications, such as acetylation and phosphorylation, suggesting that BRDs recognize combinations of marks rather than singly acetylated sequences. We further uncovered a structural mechanism for the simultaneous binding and recognition of diverse diacetyl-containing peptides by BRD4. These data provide a foundation for structure-based drug design of specific inhibitors for this emerging target family.

Authors : Filippakopoulos Panagis , Picaud Sarah , Mangos Maria , Keates Tracy , Lambert Jean-Philippe , Barsyte-Lovejoy Dalia , Felletar Ildiko , Volkmer Rudolf , Müller Susanne , Pawson Tony , Gingras Anne-Claude , Arrowsmith Cheryl H , Knapp Stefan ,

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