| http://purl.uniprot.org/citations/22464331 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22464331 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22464331 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2012.02.013"xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2012.02.013"xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Arrowsmith C.H."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Arrowsmith C.H."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Knapp S."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Knapp S."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Gingras A.C."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Gingras A.C."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Muller S."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Muller S."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Pawson T."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Pawson T."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Lambert J.P."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Lambert J.P."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Volkmer R."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Volkmer R."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Mangos M."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Mangos M."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Picaud S."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Picaud S."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Barsyte-Lovejoy D."xsd:string |
| http://purl.uniprot.org/citations/22464331 | http://purl.uniprot.org/core/author | "Barsyte-Lovejoy D."xsd:string |