2vd7
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal Structure of JMJD2A complexed with inhibitor Pyridine-2,4- dicarboxylic acid== | |
- | + | <StructureSection load='2vd7' size='340' side='right' caption='[[2vd7]], [[Resolution|resolution]] 2.25Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[2vd7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VD7 FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PD2:PYRIDINE-2,4-DICARBOXYLIC+ACID'>PD2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gp3|2gp3]], [[2gfa|2gfa]], [[2gp5|2gp5]], [[2gf7|2gf7]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vd7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vd7 RCSB], [http://www.ebi.ac.uk/pdbsum/2vd7 PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vd/2vd7_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The 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<ref>PMID:18942826</ref> | |
- | + | ||
- | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | + | </div> | |
+ | |||
+ | ==See Also== | ||
+ | *[[Jumonji domain-containing protein 2A|Jumonji domain-containing protein 2A]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Arrowsmith, C H.]] | [[Category: Arrowsmith, C H.]] |
Revision as of 05:21, 3 October 2014
Crystal Structure of JMJD2A complexed with inhibitor Pyridine-2,4- dicarboxylic acid
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Categories: Human | 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