2vd7
Crystal Structure of JMJD2A complexed with inhibitor Pyridine-2,4- dicarboxylic acidCrystal Structure of JMJD2A complexed with inhibitor Pyridine-2,4- dicarboxylic acid
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe dynamic methylation of histone lysyl residues plays an important role in biology by regulating transcription, maintaining genomic integrity, and by contributing to epigenetic effects. Here we describe a variety of inhibitor scaffolds that inhibit the human 2-oxoglutarate-dependent JMJD2 subfamily of histone demethylases. Combined with structural data, these chemical starting points will be useful to generate small-molecule probes to analyze the physiological roles of these enzymes in epigenetic signaling. Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases.,Rose NR, Ng SS, Mecinovic J, Lienard BM, Bello SH, Sun Z, McDonough MA, Oppermann U, Schofield CJ J Med Chem. 2008 Nov 27;51(22):7053-6. doi: 10.1021/jm800936s. PMID:18942826[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Human
- Large Structures
- Arrowsmith, C H
- Delft, F von
- Edwards, A
- Kavanagh, K L
- McDonough, M A
- Ng, S S
- Oppermann, U
- Pilka, E S
- Savitsky, P
- Schofield, C J
- Sundstrom, M
- Weigelt, J
- Chromatin regulator
- Dioxygenase
- Histone demethylation inhibitor jmjc domain
- Host-virus interaction
- Iron
- Metal-binding
- Nucleus
- Oxidoreductase
- Phosphorylation
- Transcription
- Transcription regulation
- Zinc-finger