4QC3
Crystal structure of human BAZ2B bromodomain in complex with a diacetylated histone 4 peptide (H4K8acK12ac)
Summary for 4QC3
| Entry DOI | 10.2210/pdb4qc3/pdb |
| Related | 4QBM 4QC1 |
| Descriptor | Bromodomain adjacent to zinc finger domain protein 2B, diacetylated histone 4 peptide (H4K8acK12ac), 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | bromodomain adjacent to zinc finger domain protein 2b, hwalp4, kiaa1476, transcriptional regulation, structural genomics consortium, sgc, transcription |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus : Q9UIF8 |
| Total number of polymer chains | 3 |
| Total formula weight | 25864.60 |
| Authors | Tallant, C.,Jose, B.,Picaud, S.,Chaikuad, A.,Filippakopoulos, P.,Burgess-Brown, N.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.M.,Bountra, C.,Knapp, S.,Structural Genomics Consortium (SGC) (deposition date: 2014-05-09, release date: 2014-05-21, Last modification date: 2023-12-06) |
| Primary citation | Tallant, C.,Valentini, E.,Fedorov, O.,Overvoorde, L.,Ferguson, F.M.,Filippakopoulos, P.,Svergun, D.I.,Knapp, S.,Ciulli, A. Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC. Structure, 23:80-92, 2015 Cited by PubMed Abstract: Binding of the chromatin remodeling complex NoRC to RNA complementary to the rDNA promoter mediates transcriptional repression. TIP5, the largest subunit of NoRC, is involved in recruitment to rDNA by interactions with promoter-bound TTF-I, pRNA, and acetylation of H4K16. TIP5 domains that recognize posttranslational modifications on histones are essential for recruitment of NoRC to chromatin, but how these reader modules recognize site-specific histone tails has remained elusive. Here, we report crystal structures of PHD zinc finger and bromodomains from human TIP5 and BAZ2B in free form and bound to H3 and/or H4 histones. PHD finger functions as an independent structural module in recognizing unmodified H3 histone tails, and the bromodomain prefers H3 and H4 acetylation marks followed by a key basic residue, KacXXR. Further low-resolution analyses of PHD-bromodomain modules provide molecular insights into their trans histone tail recognition, required for nucleosome recruitment and transcriptional repression of the NoRC complex. PubMed: 25533489DOI: 10.1016/j.str.2014.10.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report
