8SDX
ATAD2B bromodomain in complex with histone H4 acetylated at lysine 5 with Serine 1 mutation to Cysteine
Summary for 8SDX
| Entry DOI | 10.2210/pdb8sdx/pdb |
| Descriptor | ATPase family AAA domain-containing protein 2B, histone H4S1CK5ac, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | bromodomains, epigenetics, chromatin reader domain, protein binding, nuclear protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 34443.39 |
| Authors | Phillips, M.,Montgomery, C.,Nix, J.C.,Glass, K.C. (deposition date: 2023-04-07, release date: 2024-06-05, Last modification date: 2024-11-13) |
| Primary citation | Phillips, M.,Malone, K.L.,Boyle, B.W.,Montgomery, C.,Kressy, I.A.,Joseph, F.M.,Bright, K.M.,Boyson, S.P.,Chang, S.,Nix, J.C.,Young, N.L.,Jeffers, V.,Frietze, S.,Glass, K.C. Impact of Combinatorial Histone Modifications on Acetyllysine Recognition by the ATAD2 and ATAD2B Bromodomains. J.Med.Chem., 67:8186-8200, 2024 Cited by PubMed Abstract: The ATPase family AAA domain containing 2 (ATAD2) protein and its paralog ATAD2B have a C-terminal bromodomain (BRD) that functions as a reader of acetylated lysine residues on histone proteins. Using a structure-function approach, we investigated the ability of the ATAD2/B BRDs to select acetylated lysine among multiple histone post-translational modifications. The ATAD2B BRD can bind acetylated histone ligands that also contain adjacent methylation or phosphorylation marks, while the presence of these modifications significantly weakened the acetyllysine binding activity of the ATAD2 BRD. Our structural studies provide mechanistic insights into how ATAD2/B BRD-binding pocket residues coordinate the acetyllysine group in the context of adjacent post-translational modifications. Furthermore, we investigated how sequence changes in amino acids of the histone ligands impact the recognition of an adjacent acetyllysine residue. Our study highlights how the interplay between multiple combinations of histone modifications influences the reader activity of the ATAD2/B BRDs, resulting in distinct binding modes. PubMed: 38733345DOI: 10.1021/acs.jmedchem.4c00210 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.69 Å) |
Structure validation
Download full validation report
