3UV5
Crystal Structure of the tandem bromodomains of human Transcription initiation factor TFIID subunit 1 (TAF1)
Summary for 3UV5
| Entry DOI | 10.2210/pdb3uv5/pdb |
| Related | 3UV2 3UV4 3UVD 3UVW 3UVX 3UVY 3UW9 |
| Descriptor | Transcription initiation factor TFIID subunit 1, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total) |
| Functional Keywords | tandem bromodomain, taf1, cell cycle gene 1 protein, tbp-associated factor 250 kda, transcription initiation factor tfiid 250 kda subunit, tfii-250, structural genomics consortium, sgc, transcription |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P21675 |
| Total number of polymer chains | 1 |
| Total formula weight | 31090.40 |
| Authors | Filippakopoulos, P.,Felletar, I.,Picaud, S.,Keates, T.,Muniz, J.,Gileadi, O.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.M.,Weigelt, J.,Bountra, C.,Knapp, S.,Structural Genomics Consortium (SGC) (deposition date: 2011-11-29, release date: 2012-01-18, Last modification date: 2024-10-30) |
| Primary citation | Filippakopoulos, P.,Picaud, S.,Mangos, M.,Keates, T.,Lambert, J.P.,Barsyte-Lovejoy, D.,Felletar, I.,Volkmer, R.,Muller, S.,Pawson, T.,Gingras, A.C.,Arrowsmith, C.H.,Knapp, S. Histone recognition and large-scale structural analysis of the human bromodomain family. Cell(Cambridge,Mass.), 149:214-231, 2012 Cited by PubMed Abstract: 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. PubMed: 22464331DOI: 10.1016/j.cell.2012.02.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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