4nvq
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4nvq is ON HOLD Authors: Sweis, R.F., Pliushchev, M., Brown, P.J., Guo, J., Li, F., Maag, D., Petros, A.M., Soni, N.B., Tse, C., Vedadi, M., Michael...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Human G9a in Complex with Inhibitor A-366== | |
| + | <StructureSection load='4nvq' size='340' side='right'caption='[[4nvq]], [[Resolution|resolution]] 2.03Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4nvq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NVQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2OD:5-METHOXY-6-[3-(PYRROLIDIN-1-YL)PROPOXY]SPIRO[CYCLOBUTANE-1,3-INDOL]-2-AMINE'>2OD</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nvq OCA], [https://pdbe.org/4nvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nvq RCSB], [https://www.ebi.ac.uk/pdbsum/4nvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nvq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/EHMT2_HUMAN EHMT2_HUMAN] Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.<ref>PMID:8457211</ref> <ref>PMID:11316813</ref> <ref>PMID:18438403</ref> <ref>PMID:20118233</ref> <ref>PMID:22387026</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Brown PJ]] | ||
| + | [[Category: Chiang GG]] | ||
| + | [[Category: Guo J]] | ||
| + | [[Category: Li F]] | ||
| + | [[Category: Maag D]] | ||
| + | [[Category: Michaelides MR]] | ||
| + | [[Category: Pappano WN]] | ||
| + | [[Category: Petros AM]] | ||
| + | [[Category: Pliushchev M]] | ||
| + | [[Category: Soni NB]] | ||
| + | [[Category: Sweis RF]] | ||
| + | [[Category: Tse C]] | ||
| + | [[Category: Vedadi M]] | ||
Current revision
Human G9a in Complex with Inhibitor A-366
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Categories: Homo sapiens | Large Structures | Brown PJ | Chiang GG | Guo J | Li F | Maag D | Michaelides MR | Pappano WN | Petros AM | Pliushchev M | Soni NB | Sweis RF | Tse C | Vedadi M
