3TLP
Crystal structure of the fourth bromodomain of human poly-bromodomain containing protein 1 (PB1)
Summary for 3TLP
| Entry DOI | 10.2210/pdb3tlp/pdb |
| Descriptor | Protein polybromo-1, NICKEL (II) ION (3 entities in total) |
| Functional Keywords | pb1, polybromo 1 isoform 1, baf180, polybromo-1d, pbrm1, brg1-associated factor 180, structural genomics consortium, sgc, bromodomain, transcription |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q86U86 |
| Total number of polymer chains | 2 |
| Total formula weight | 35162.94 |
| Authors | Filippakopoulos, P.,Felletar, I.,Picaud, S.,Keates, T.,Muniz, J.,Krojer, T.,Allerston, C.K.,Latwiel, S.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.M.,Weigelt, J.,Bountra, C.,Knapp, S.,Structural Genomics Consortium (SGC) (deposition date: 2011-08-30, release date: 2011-09-28, Last modification date: 2023-09-13) |
| 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 (2.13 Å) |
Structure validation
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