5EIS
FIRST DOMAIN OF HUMAN BROMODOMAIN BRD4 IN COMPLEX WITH INHIBITOR 3-(4-Chlorobenzyl)-7-ethyl-3,7-dihydropurine-2,6-dione
Summary for 5EIS
Entry DOI | 10.2210/pdb5eis/pdb |
Descriptor | Bromodomain-containing protein 4, 3-[(4-chlorophenyl)methyl]-7-ethyl-purine-2,6-dione, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | inhibitor, histone, epigenetic reader, bromodomain, brd4_bd1, transcription |
Biological source | Homo sapiens (Human) More |
Cellular location | Nucleus: O60885 |
Total number of polymer chains | 1 |
Total formula weight | 15528.25 |
Authors | Raux, B.,Rebuffet, E.,Betzi, S.,Morelli, X. (deposition date: 2015-10-30, release date: 2016-01-20, Last modification date: 2024-01-10) |
Primary citation | Raux, B.,Voitovich, Y.,Derviaux, C.,Lugari, A.,Rebuffet, E.,Milhas, S.,Priet, S.,Roux, T.,Trinquet, E.,Guillemot, J.C.,Knapp, S.,Brunel, J.M.,Fedorov, A.Y.,Collette, Y.,Roche, P.,Betzi, S.,Combes, S.,Morelli, X. Exploring Selective Inhibition of the First Bromodomain of the Human Bromodomain and Extra-terminal Domain (BET) Proteins. J.Med.Chem., 59:1634-1641, 2016 Cited by PubMed Abstract: A midthroughput screening follow-up program targeting the first bromodomain of the human BRD4 protein, BRD4(BD1), identified an acetylated-mimic xanthine derivative inhibitor. This compound binds with an affinity in the low micromolar range yet exerts suitable unexpected selectivity in vitro against the other members of the bromodomain and extra-terminal domain (BET) family. A structure-based program pinpointed a role of the ZA loop, paving the way for the development of potent and selective BET-BRDi probes. PubMed: 26735842DOI: 10.1021/acs.jmedchem.5b01708 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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