3rjw
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3rjw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3nni 3nni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RJW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RJW FirstGlance]. <br> | <table><tr><td colspan='2'>[[3rjw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3nni 3nni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RJW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RJW FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIQ:2-CYCLOHEXYL-6-METHOXY-N-[1-(1-METHYLETHYL)PIPERIDIN-4-YL]-7-(3-PYRROLIDIN-1-YLPROPOXY)QUINAZOLIN-4-AMINE'>CIQ</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIQ:2-CYCLOHEXYL-6-METHOXY-N-[1-(1-METHYLETHYL)PIPERIDIN-4-YL]-7-(3-PYRROLIDIN-1-YLPROPOXY)QUINAZOLIN-4-AMINE'>CIQ</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHMT2, BAT8, C6orf30, G9A, KMT1C, NG36 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHMT2, BAT8, C6orf30, G9A, KMT1C, NG36 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></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=3rjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rjw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rjw RCSB], [http://www.ebi.ac.uk/pdbsum/3rjw PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rjw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rjw RCSB], [http://www.ebi.ac.uk/pdbsum/3rjw PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 14: | Line 16: | ||
A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells.,Vedadi M, Barsyte-Lovejoy D, Liu F, Rival-Gervier S, Allali-Hassani A, Labrie V, Wigle TJ, Dimaggio PA, Wasney GA, Siarheyeva A, Dong A, Tempel W, Wang SC, Chen X, Chau I, Mangano TJ, Huang XP, Simpson CD, Pattenden SG, Norris JL, Kireev DB, Tripathy A, Edwards A, Roth BL, Janzen WP, Garcia BA, Petronis A, Ellis J, Brown PJ, Frye SV, Arrowsmith CH, Jin J Nat Chem Biol. 2011 Jul 10;7(8):566-74. doi: 10.1038/nchembio.599. PMID:21743462<ref>PMID:21743462</ref> | A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells.,Vedadi M, Barsyte-Lovejoy D, Liu F, Rival-Gervier S, Allali-Hassani A, Labrie V, Wigle TJ, Dimaggio PA, Wasney GA, Siarheyeva A, Dong A, Tempel W, Wang SC, Chen X, Chau I, Mangano TJ, Huang XP, Simpson CD, Pattenden SG, Norris JL, Kireev DB, Tripathy A, Edwards A, Roth BL, Janzen WP, Garcia BA, Petronis A, Ellis J, Brown PJ, Frye SV, Arrowsmith CH, Jin J Nat Chem Biol. 2011 Jul 10;7(8):566-74. doi: 10.1038/nchembio.599. PMID:21743462<ref>PMID:21743462</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| Line 25: | Line 27: | ||
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Allali-Hassani, A | + | [[Category: Allali-Hassani, A]] |
| - | [[Category: Arora, K | + | [[Category: Arora, K]] |
| - | [[Category: Arrowsmith, C H | + | [[Category: Arrowsmith, C H]] |
| - | [[Category: Barsyte, D | + | [[Category: Barsyte, D]] |
| - | [[Category: Bochkarev, A | + | [[Category: Bochkarev, A]] |
| - | [[Category: Bountra, C | + | [[Category: Bountra, C]] |
| - | [[Category: Brown, P J | + | [[Category: Brown, P J]] |
| - | [[Category: Chau, I | + | [[Category: Chau, I]] |
| - | [[Category: Chavda, N | + | [[Category: Chavda, N]] |
| - | [[Category: Chen, X | + | [[Category: Chen, X]] |
| - | [[Category: Dong, A | + | [[Category: Dong, A]] |
| - | [[Category: Edwards, A M | + | [[Category: Edwards, A M]] |
| - | [[Category: Frye, S V | + | [[Category: Frye, S V]] |
| - | [[Category: Hajian, T | + | [[Category: Hajian, T]] |
| - | [[Category: Herold, J M | + | [[Category: Herold, J M]] |
| - | [[Category: Jin, J | + | [[Category: Jin, J]] |
| - | [[Category: Kireev, D B | + | [[Category: Kireev, D B]] |
| - | [[Category: Liu, F | + | [[Category: Liu, F]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Senisterra, G | + | [[Category: Senisterra, G]] |
| - | [[Category: Siarheyeva, A | + | [[Category: Siarheyeva, A]] |
| - | [[Category: Tempel, W | + | [[Category: Tempel, W]] |
| - | [[Category: Vedadi, M | + | [[Category: Vedadi, M]] |
| - | [[Category: Wasney, G A | + | [[Category: Wasney, G A]] |
| - | [[Category: Weigelt, J | + | [[Category: Weigelt, J]] |
[[Category: Chemical probe]] | [[Category: Chemical probe]] | ||
[[Category: Methyltransferase inhibitor]] | [[Category: Methyltransferase inhibitor]] | ||
[[Category: Sgc]] | [[Category: Sgc]] | ||
| - | [[Category: Structural genomics consortium]] | ||
[[Category: Transferase-transferase inhibitor complex]] | [[Category: Transferase-transferase inhibitor complex]] | ||
Revision as of 17:57, 25 December 2014
Crystal structure of histone lysine methyltransferase g9a with an inhibitor
| |||||||||||
Categories: Histone-lysine N-methyltransferase | Homo sapiens | Allali-Hassani, A | Arora, K | Arrowsmith, C H | Barsyte, D | Bochkarev, A | Bountra, C | Brown, P J | Chau, I | Chavda, N | Chen, X | Dong, A | Edwards, A M | Frye, S V | Hajian, T | Herold, J M | Jin, J | Kireev, D B | Liu, F | Structural genomic | Senisterra, G | Siarheyeva, A | Tempel, W | Vedadi, M | Wasney, G A | Weigelt, J | Chemical probe | Methyltransferase inhibitor | Sgc | Transferase-transferase inhibitor complex
