3NJY
Crystal structure of JMJD2A complexed with 5-carboxy-8-hydroxyquinoline
Summary for 3NJY
| Entry DOI | 10.2210/pdb3njy/pdb |
| Related | 2GF7 2GFA 2GP3 2GP5 2VD7 2WWJ |
| Descriptor | Lysine-specific demethylase 4A, NICKEL (II) ION, ZINC ION, ... (5 entities in total) |
| Functional Keywords | oxidoreductase, chromatin regulator, transcription regulation, double-stranded beta helix, oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: O75164 |
| Total number of polymer chains | 2 |
| Total formula weight | 89279.08 |
| Authors | King, O.N.F.,Clifton, I.J.,Wang, M.,Maloney, D.J.,Jadhav, A.,Oppermann, U.,Heightman, T.D.,Simeonov, A.,McDonough, M.A.,Schofield, C.J. (deposition date: 2010-06-18, release date: 2010-12-08, Last modification date: 2023-11-01) |
| Primary citation | King, O.N.F.,Li, X.S.,Sakurai, M.,Kawamura, A.,Rose, N.R.,Ng, S.S.,Quinn, A.M.,Rai, G.,Mott, B.T.,Beswick, P.,Klose, R.J.,Oppermann, U.,Jadhav, A.,Heightman, T.D.,Maloney, D.J.,Schofield, C.J.,Simeonov, A. Quantitative high-throughput screening identifies 8-hydroxyquinolines as cell-active histone demethylase inhibitors Plos One, 5:e15535-e15535, 2010 Cited by PubMed Abstract: Small molecule modulators of epigenetic processes are currently sought as basic probes for biochemical mechanisms, and as starting points for development of therapeutic agents. N(ε)-Methylation of lysine residues on histone tails is one of a number of post-translational modifications that together enable transcriptional regulation. Histone lysine demethylases antagonize the action of histone methyltransferases in a site- and methylation state-specific manner. N(ε)-Methyllysine demethylases that use 2-oxoglutarate as co-factor are associated with diverse human diseases, including cancer, inflammation and X-linked mental retardation; they are proposed as targets for the therapeutic modulation of transcription. There are few reports on the identification of templates that are amenable to development as potent inhibitors in vivo and large diverse collections have yet to be exploited for the discovery of demethylase inhibitors. PubMed: 21124847DOI: 10.1371/journal.pone.0015535 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report
