4IOO
Crystal Structure of the first bromodomain of BRD4 in complex with N-methyltrimethylacetamide
Summary for 4IOO
| Entry DOI | 10.2210/pdb4ioo/pdb |
| Related | 4IOQ 4IOR |
| Descriptor | Bromodomain-containing protein 4, 1,2-ETHANEDIOL, N-methyltrimethylacetamide, ... (5 entities in total) |
| Functional Keywords | bromodomain, low mw fragment, dna binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: O60885 |
| Total number of polymer chains | 1 |
| Total formula weight | 15603.03 |
| Authors | Lolli, G.,Battistutta, R. (deposition date: 2013-01-08, release date: 2013-10-02, Last modification date: 2024-02-28) |
| Primary citation | Lolli, G.,Battistutta, R. Different orientations of low-molecular-weight fragments in the binding pocket of a BRD4 bromodomain. Acta Crystallogr.,Sect.D, 69:2161-2164, 2013 Cited by PubMed Abstract: Bromodomains are involved in the regulation of chromatin architecture and transcription through the recognition of acetylated lysines in histones and other proteins. Many of them are considered to be relevant pharmacological targets for different pathologies. Three crystallographic structures of the N-terminal bromodomain of BRD4 in complex with low-molecular-weight fragments are presented. They show that similar molecules mimicking acetylated lysine bind the bromodomain with different orientations and exploit different interactions. It is also advised to avoid DMSO when searching for low-affinity fragments that interact with bromodomains since DMSO binds in the acetylated lysine-recognition pocket of BRD4. PubMed: 24100334DOI: 10.1107/S090744491301994X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.25 Å) |
Structure validation
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