3mo2 - Revision history

OCA at 08:57, 6 September 2023

2023-09-06T08:57:25Z

← Older revision		Revision as of 08:57, 6 September 2023
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	==human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67==		==human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67==
	<StructureSection load='3mo2' size='340' side='right' caption='[[3mo2]], [[Resolution\|resolution]] 2.49Å' scene=''>		<StructureSection load='3mo2' size='340' side='right'caption='[[3mo2]], [[Resolution\|resolution]] 2.49Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3mo2]] is a 4 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=3MO2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3MO2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3mo2]] is a 4 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=3MO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MO2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E67:7-[(5-AMINOPENTYL)OXY]-N~4~-(1-BENZYLPIPERIDIN-4-YL)-N~2~-[3-(DIMETHYLAMINO)PROPYL]-6-METHOXYQUINAZOLINE-2,4-DIAMINE'>E67</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.49Å</td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3fpd\|3fpd]], [[3mo0\|3mo0]], [[3mo5\|3mo5]]</td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E67:7-[(5-AMINOPENTYL)OXY]-N~4~-(1-BENZYLPIPERIDIN-4-YL)-N~2~-[3-(DIMETHYLAMINO)PROPYL]-6-METHOXYQUINAZOLINE-2,4-DIAMINE'>E67</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EHMT1, EUHMTASE1, KIAA1876, KMT1D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3mo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mo2 OCA], [https://pdbe.org/3mo2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mo2 RCSB], [https://www.ebi.ac.uk/pdbsum/3mo2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mo2 ProSAT]</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 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=3mo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mo2 OCA], [~~http~~://pdbe.org/3mo2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3mo2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3mo2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3mo2 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[~~[http~~://www.uniprot.org/uniprot/EHMT1_HUMAN EHMT1_HUMAN]] Defects in EHMT1 are the cause of chromosome 9q subtelomeric deletion syndrome (9q- syndrome) [MIM:[~~http~~://omim.org/entry/610253 610253]]. Common features seen in these patients are severe mental retardation, hypotonia, brachy(micro)cephaly, epileptic seizures, flat face with hypertelorism, synophrys, anteverted nares, cupid bow or tented upper lip, everted lower lip, prognathism, macroglossia, conotruncal heart defects, and behavioral problems.		[https://www.uniprot.org/uniprot/EHMT1_HUMAN EHMT1_HUMAN] Defects in EHMT1 are the cause of chromosome 9q subtelomeric deletion syndrome (9q- syndrome) [MIM:[https://omim.org/entry/610253 610253]. Common features seen in these patients are severe mental retardation, hypotonia, brachy(micro)cephaly, epileptic seizures, flat face with hypertelorism, synophrys, anteverted nares, cupid bow or tented upper lip, everted lower lip, prognathism, macroglossia, conotruncal heart defects, and behavioral problems.
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/EHMT1_HUMAN EHMT1_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 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. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53.<ref>PMID:12004135</ref> <ref>PMID:20118233</ref>		[https://www.uniprot.org/uniprot/EHMT1_HUMAN EHMT1_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 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. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53.<ref>PMID:12004135</ref> <ref>PMID:20118233</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
	*[[Histone methyltransferase\|Histone methyltransferase]]		*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Histone-lysine N-methyltransferase~~]]		[[Category: Homo sapiens]]
	[[Category: ~~Human~~]]		[[Category: Large Structures]]
	[[Category: Chang, Y]]		[[Category: Chang Y]]
	[[Category: Cheng, X]]		[[Category: Cheng X]]
	[[Category: Horton~~, J R]]~~		[[Category: Horton JR]]
	~~[[Category: Enzymatic inhibition]]~~
	~~[[Category: Epigenetic]]~~
	~~[[Category: Histone lysine methylation]]~~
	~~[[Category: Lysine mimic]]~~
	~~[[Category: Transferase~~]]

OCA at 13:35, 16 January 2019

2019-01-16T13:35:19Z

← Older revision		Revision as of 13:35, 16 January 2019
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/3mo2_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/3mo2_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 18:47, 4 August 2016

2016-08-04T18:47:19Z

← Older revision		Revision as of 18:47, 4 August 2016
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	==human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67==		==human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67==
	<StructureSection load='3mo2' size='340' side='right' caption='[[3mo2]], [[Resolution\|resolution]] 2.49Å' scene=''>		<StructureSection load='3mo2' size='340' side='right' caption='[[3mo2]], [[Resolution\|resolution]] 2.49Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3mo2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MO2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MO2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3mo2]] is a 4 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=3MO2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MO2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E67:7-[(5-AMINOPENTYL)OXY]-N~4~-(1-BENZYLPIPERIDIN-4-YL)-N~2~-[3-(DIMETHYLAMINO)PROPYL]-6-METHOXYQUINAZOLINE-2,4-DIAMINE'>E67</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E67:7-[(5-AMINOPENTYL)OXY]-N~4~-(1-BENZYLPIPERIDIN-4-YL)-N~2~-[3-(DIMETHYLAMINO)PROPYL]-6-METHOXYQUINAZOLINE-2,4-DIAMINE'>E67</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3fpd\|3fpd]], [[3mo0\|3mo0]], [[3mo5\|3mo5]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3fpd\|3fpd]], [[3mo0\|3mo0]], [[3mo5\|3mo5]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EHMT1, EUHMTASE1, KIAA1876, KMT1D ([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">EHMT1, EUHMTASE1, KIAA1876, KMT1D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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 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 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=3mo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mo2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mo2 RCSB], [http://www.ebi.ac.uk/pdbsum/3mo2 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=3mo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mo2 OCA], [http://pdbe.org/3mo2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mo2 RCSB], [http://www.ebi.ac.uk/pdbsum/3mo2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mo2 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</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].		</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/main_output.php?pdb_ID=3mo2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 3mo2" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	</StructureSection>		</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Chang, Y]]		[[Category: Chang, Y]]
	[[Category: Cheng, X]]		[[Category: Cheng, X]]

OCA at 16:23, 18 December 2014

2014-12-18T16:23:14Z

← Older revision		Revision as of 16:23, 18 December 2014
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	~~{{STRUCTURE_3mo2\| PDB=3mo2 \| SCENE= }}~~		==human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67==
	===human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67===		<StructureSection load='3mo2' size='340' side='right' caption='[[3mo2]], [[Resolution\|resolution]] 2.49Å' scene=''>
	~~{{ABSTRACT_PUBMED_20434463}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[3mo2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MO2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MO2 FirstGlance]. <br>
	==Disease==		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E67:7-[(5-AMINOPENTYL)OXY]-N~4~-(1-BENZYLPIPERIDIN-4-YL)-N~2~-[3-(DIMETHYLAMINO)PROPYL]-6-METHOXYQUINAZOLINE-2,4-DIAMINE'>E67</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3fpd\|3fpd]], [[3mo0\|3mo0]], [[3mo5\|3mo5]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EHMT1, EUHMTASE1, KIAA1876, KMT1D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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 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=3mo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mo2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mo2 RCSB], [http://www.ebi.ac.uk/pdbsum/3mo2 PDBsum]</span></td></tr>
			</table>
			== Disease ==
	[[http://www.uniprot.org/uniprot/EHMT1_HUMAN EHMT1_HUMAN]] Defects in EHMT1 are the cause of chromosome 9q subtelomeric deletion syndrome (9q- syndrome) [MIM:[http://omim.org/entry/610253 610253]]. Common features seen in these patients are severe mental retardation, hypotonia, brachy(micro)cephaly, epileptic seizures, flat face with hypertelorism, synophrys, anteverted nares, cupid bow or tented upper lip, everted lower lip, prognathism, macroglossia, conotruncal heart defects, and behavioral problems.		[[http://www.uniprot.org/uniprot/EHMT1_HUMAN EHMT1_HUMAN]] Defects in EHMT1 are the cause of chromosome 9q subtelomeric deletion syndrome (9q- syndrome) [MIM:[http://omim.org/entry/610253 610253]]. Common features seen in these patients are severe mental retardation, hypotonia, brachy(micro)cephaly, epileptic seizures, flat face with hypertelorism, synophrys, anteverted nares, cupid bow or tented upper lip, everted lower lip, prognathism, macroglossia, conotruncal heart defects, and behavioral problems.
			== Function ==
			[[http://www.uniprot.org/uniprot/EHMT1_HUMAN EHMT1_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 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. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53.<ref>PMID:12004135</ref> <ref>PMID:20118233</ref>
			== 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/mo/3mo2_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 ==
			Dynamic histone lysine methylation involves the activities of modifying enzymes (writers), enzymes removing modifications (erasers), and readers of the histone code. One common feature of these activities is the recognition of lysines in methylated and unmethylated states, whether they are substrates, reaction products, or binding partners. We applied the concept of adding a lysine mimic to an established inhibitor (BIX-01294) of histone H3 lysine 9 methyltransferases G9a and G9a-like protein by including a 5-aminopentyloxy moiety, which is inserted into the target lysine-binding channel and becomes methylated by G9a-like protein, albeit slowly. The compound enhances its potency in vitro and reduces cell toxicity in vivo. We suggest that adding a lysine or methyl-lysine mimic should be considered in the design of small-molecule inhibitors for other methyl-lysine writers, erasers, and readers.

	~~==Function==~~		Adding a lysine mimic in the design of potent inhibitors of histone lysine methyltransferases.,Chang Y, Ganesh T, Horton JR, Spannhoff A, Liu J, Sun A, Zhang X, Bedford MT, Shinkai Y, Snyder JP, Cheng X J Mol Biol. 2010 Jul 2;400(1):1-7. Epub 2010 Apr 29. PMID:20434463<ref>PMID:20434463</ref>
	~~[[http://www.uniprot.org/uniprot/EHMT1_HUMAN EHMT1_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 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. During G0 phase~~, ~~it probably contributes to silencing of MYC- and E2F-responsive genes~~, ~~suggesting a role in G0/G1 transition in cell cycle~~. ~~In addition to the histone methyltransferase activity, also methylates non-histone proteins~~: ~~mediates dimethylation of 'Lys~~-~~373' of p53/TP53~~.~~<ref>~~PMID:~~12004135</ref>~~<ref>PMID:~~20118233~~</ref>

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[3mo2]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:/~~/~~oca.weizmann.ac.il/oca-bin/ocashort?id=3MO2 OCA].~~		</div>

	==~~Reference~~==		==See Also==
	~~<ref group~~=~~"xtra">PMID:020434463</ref>~~<references ~~group="xtra"~~/><~~references~~/>		*[[Histone methyltransferase\|Histone methyltransferase]]
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chang, Y.]]		[[Category: Chang, Y]]
	[[Category: Cheng, X.]]		[[Category: Cheng, X]]
	[[Category: Horton, J R.]]		[[Category: Horton, J R]]
	[[Category: Enzymatic inhibition]]		[[Category: Enzymatic inhibition]]
	[[Category: Epigenetic]]		[[Category: Epigenetic]]

OCA: Protected "3mo2" [edit=sysop:move=sysop]

2013-03-25T00:40:18Z

Protected "3mo2" [edit=sysop:move=sysop]

← Older revision	Revision as of 00:40, 25 March 2013
(No difference)

OCA at 00:40, 25 March 2013

2013-03-25T00:40:16Z

← Older revision		Revision as of 00:40, 25 March 2013
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	~~{{Seed}}~~
	~~[[Image:3mo2.jpg\|left\|200px]]~~

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3mo2", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
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	{{STRUCTURE_3mo2\| PDB=3mo2 \| SCENE= }}		{{STRUCTURE_3mo2\| PDB=3mo2 \| SCENE= }}

	===human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67===		===human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67===
			{{ABSTRACT_PUBMED_20434463}}

			==Disease==
			[[http://www.uniprot.org/uniprot/EHMT1_HUMAN EHMT1_HUMAN]] Defects in EHMT1 are the cause of chromosome 9q subtelomeric deletion syndrome (9q- syndrome) [MIM:[http://omim.org/entry/610253 610253]]. Common features seen in these patients are severe mental retardation, hypotonia, brachy(micro)cephaly, epileptic seizures, flat face with hypertelorism, synophrys, anteverted nares, cupid bow or tented upper lip, everted lower lip, prognathism, macroglossia, conotruncal heart defects, and behavioral problems.

	~~<!--~~		==Function==
	~~The line below this paragraph, {{ABSTRACT_PUBMED_20434463}}, adds the Publication Abstract to the page~~		[[http://www.uniprot.org/uniprot/EHMT1_HUMAN EHMT1_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 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. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53.<ref>PMID:12004135</ref><ref>PMID:20118233</ref>
	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov~~), ~~where 20434463~~ is the ~~PubMed ID number.~~
	-->
	~~{{ABSTRACT_PUBMED_20434463}}~~

	==About this Structure==		==About this Structure==
	~~3MO2~~ is a 4 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MO2 OCA].		[[3mo2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MO2 OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~20434463~~</ref><references group="xtra"/>		<ref group="xtra">PMID:020434463</ref><references group="xtra"/><references/>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 34:		Line 24:
	[[Category: Lysine mimic]]		[[Category: Lysine mimic]]
	[[Category: Transferase]]		[[Category: Transferase]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 30 13:49:19 2010''~~

OCA at 09:43, 30 June 2010

2010-06-30T09:43:45Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{Seed}}
-The entry 3mo2 is ON HOLD
+<!--
-Authors: Chang, Y., Horton, J.R., Cheng, X.
+===human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67===
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May  5 11:41:03 2010''
+<!--

OCA: New page: '''Unreleased structure''' The entry 3mo2 is ON HOLD Authors: Chang, Y., Horton, J.R., Cheng, X. Description: human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67 '...

2010-05-05T08:41:03Z

New page: '''Unreleased structure''' The entry 3mo2 is ON HOLD Authors: Chang, Y., Horton, J.R., Cheng, X. Description: human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67 '...

New page

'''Unreleased structure'''

The entry 3mo2 is ON HOLD

Authors: Chang, Y., Horton, J.R., Cheng, X.

Description: human G9a-like (GLP, also known as EHMT1) in complex with inhibitor E67

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 5 11:41:03 2010''