4e47 - Revision history

OCA at 14:52, 14 March 2024

2024-03-14T14:52:06Z

← Older revision		Revision as of 14:52, 14 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e47]] 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E47 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e47]] 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E47 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [https://pdbe.org/4e47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [https://www.ebi.ac.uk/pdbsum/4e47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e47 ProSAT]</span></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=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [https://pdbe.org/4e47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [https://www.ebi.ac.uk/pdbsum/4e47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e47 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>		[https://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>

	==See Also==		==See Also==

OCA at 06:49, 28 September 2022

2022-09-28T06:49:08Z

← Older revision		Revision as of 06:49, 28 September 2022
Line 1:		Line 1:

	==SET7/9 in complex with inhibitor (R)-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahydroisoquinoline-6- sulfonamide and S-adenosylmethionine==		==SET7/9 in complex with inhibitor (R)-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahydroisoquinoline-6- sulfonamide and S-adenosylmethionine==
	<StructureSection load='4e47' size='340' side='right' caption='[[4e47]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4e47' size='340' side='right'caption='[[4e47]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e47]] 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4E47 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e47]] 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E47 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SETD7, KIAA1717, KMT7, SET7, SET9 ([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=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [https://pdbe.org/4e47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [https://www.ebi.ac.uk/pdbsum/4e47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e47 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=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [~~http~~://pdbe.org/4e47 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4e47 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4e47 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>		[[https://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>

			==See Also==
			*[[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: Arrowsmith~~, C H~~]]		[[Category: Arrowsmith CH]]
	[[Category: Barsyte, D]]		[[Category: Barsyte D]]
	[[Category: Bountra, C]]		[[Category: Bountra C]]
	[[Category: Brown~~, P J~~]]		[[Category: Brown PJ]]
	[[Category: Bunnage, M]]		[[Category: Bunnage M]]
	[[Category: Cook, A]]		[[Category: Cook A]]
	[[Category: Dong, A]]		[[Category: Dong A]]
	[[Category: Edwards~~, A M~~]]		[[Category: Edwards AM]]
	[[Category: Fish, P]]		[[Category: Fish P]]
	[[Category: Ouyang, H]]		[[Category: Ouyang H]]
	[[Category: Owen, D]]		[[Category: Owen D]]
	~~[[Category: Structural genomic~~]]		[[Category: Tatlock J]]
	[[Category: Tatlock, J]]		[[Category: Vedadi M]]
	[[Category: Vedadi, M]]		[[Category: Walker JR]]
	[[Category: Walker~~, J R~~]]		[[Category: Weigelt J]]
	[[Category: Weigelt, J]]
	~~[[Category: Chromatin regulator]]~~
	~~[[Category: Chromosomal protein]]~~
	~~[[Category: Inhibitor]]~~
	~~[[Category: Methyltransferase]]~~
	~~[[Category: Nucleus]]~~
	~~[[Category: S-adenosylmethionine]]~~
	~~[[Category: Set domain]]~~
	~~[[Category: Sgc]]~~
	~~[[Category: Ternary complex]]~~
	~~[[Category: Transcription]]~~
	~~[[Category: Transcription regulation]]~~
	~~[[Category: Transferase]]~~
	~~[[Category: Transferase-transferase inhibitor complex~~]]

OCA at 07:59, 15 November 2017

2017-11-15T07:59:10Z

← Older revision		Revision as of 07:59, 15 November 2017
Line 11:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>		[[http://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>

	~~==See Also==~~
	*[[Histone methyltransferase\|Histone methyltransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:24, 4 August 2016

2016-08-04T10:24:25Z

← Older revision		Revision as of 10:24, 4 August 2016
Line 1:		Line 1:

	==SET7/9 in complex with inhibitor (R)-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahydroisoquinoline-6- sulfonamide and S-adenosylmethionine==		==SET7/9 in complex with inhibitor (R)-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahydroisoquinoline-6- sulfonamide and S-adenosylmethionine==
	<StructureSection load='4e47' size='340' side='right' caption='[[4e47]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4e47' size='340' side='right' caption='[[4e47]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e47]] 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E47 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e47]] 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E47 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SETD7, KIAA1717, KMT7, SET7, SET9 ([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">SETD7, KIAA1717, KMT7, SET7, SET9 ([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=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [http://www.ebi.ac.uk/pdbsum/4e47 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=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [http://pdbe.org/4e47 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [http://www.ebi.ac.uk/pdbsum/4e47 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e47 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	</StructureSection>		</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Arrowsmith, C H]]		[[Category: Arrowsmith, C H]]
	[[Category: Barsyte, D]]		[[Category: Barsyte, D]]

OCA at 08:18, 25 December 2014

2014-12-25T08:18:53Z

← Older revision		Revision as of 08:18, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e47]] 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E47 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e47]] 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E47 FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SETD7, KIAA1717, KMT7, SET7, SET9 ([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">SETD7, KIAA1717, KMT7, SET7, SET9 ([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=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [http://www.ebi.ac.uk/pdbsum/4e47 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=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [http://www.ebi.ac.uk/pdbsum/4e47 PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>

	==See Also==		==See Also==
	*[[Histone methyltransferase\|Histone methyltransferase]]		*[[Histone methyltransferase\|Histone methyltransferase]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Arrowsmith, C H.]]		[[Category: Arrowsmith, C H]]
	[[Category: Barsyte, D.]]		[[Category: Barsyte, D]]
	[[Category: Bountra, C.]]		[[Category: Bountra, C]]
	[[Category: Brown, P J.]]		[[Category: Brown, P J]]
	[[Category: Bunnage, M.]]		[[Category: Bunnage, M]]
	[[Category: Cook, A.]]		[[Category: Cook, A]]
	[[Category: Dong, A.]]		[[Category: Dong, A]]
	[[Category: Edwards, A M.]]		[[Category: Edwards, A M]]
	[[Category: Fish, P.]]		[[Category: Fish, P]]
	[[Category: Ouyang, H.]]		[[Category: Ouyang, H]]
	[[Category: Owen, D.]]		[[Category: Owen, D]]
	[[Category: ~~SGC,~~ Structural ~~Genomics Consortium.~~]]		[[Category: Structural genomic]]
	[[Category: Tatlock, J.]]		[[Category: Tatlock, J]]
	[[Category: Vedadi, M.]]		[[Category: Vedadi, M]]
	[[Category: Walker, J R.]]		[[Category: Walker, J R]]
	[[Category: Weigelt, J.]]		[[Category: Weigelt, J]]
	[[Category: Chromatin regulator]]		[[Category: Chromatin regulator]]
	[[Category: Chromosomal protein]]		[[Category: Chromosomal protein]]
Line 39:		Line 43:
	[[Category: Set domain]]		[[Category: Set domain]]
	[[Category: Sgc]]		[[Category: Sgc]]
	~~[[Category: Structural genomics consortium]]~~
	[[Category: Ternary complex]]		[[Category: Ternary complex]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 08:01, 5 June 2014

2014-06-05T08:01:41Z

← Older revision		Revision as of 08:01, 5 June 2014
Line 1:		Line 1:
	[[~~Image~~:~~4e47~~.~~jpg~~\|~~left~~\|~~200px~~]]		==SET7/9 in complex with inhibitor (R)-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahydroisoquinoline-6- sulfonamide and S-adenosylmethionine==
			<StructureSection load='4e47' size='340' side='right' caption='[[4e47]], [[Resolution\|resolution]] 2.00Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4e47]] 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=4E47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E47 FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0N6:(R)-(3-(3-CYANOPHENYL)-1-OXO-1-(PYRROLIDIN-1-YL)PROPAN-2-YL)-1,2,3,4-TETRAHYDROISOQUINOLINE-6-SULFONAMIDE'>0N6</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SETD7, KIAA1717, KMT7, SET7, SET9 ([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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e47 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e47 RCSB], [http://www.ebi.ac.uk/pdbsum/4e47 PDBsum]</span></td></tr>
			<table>

	~~<!--~~		==See Also==
	~~The line below this paragraph, containing "STRUCTURE_4e47", creates the "Structure Box" on the page.~~		*[[Histone methyltransferase\|Histone methyltransferase]]
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~		__TOC__
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~		</StructureSection>
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	~~{{STRUCTURE_4e47\| PDB~~=~~4e47 \| SCENE= }}~~

	~~===SET7/9 in complex with inhibitor (R)-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahydroisoquinoline-6- sulfonamide and S-adenosylmethionine~~===


	~~==About this Structure==~~
	[[~~4e47~~]] ~~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=4E47 OCA].~~
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 07:54, 28 March 2012

2012-03-28T07:54:57Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:4e47.jpg|left|200px]]
-The entry 4e47 is ON HOLD
+<!--
-Authors: Walker, J.R., Ouyang, H., Dong, A., Barsyte, D., Vedadi, M., Bountra, C., Weigelt, J., Edwards, A.M., Arrowsmith, C.H., Brown, P.J., Structural Genomics Consortium (SGC)
+===SET7/9 in complex with inhibitor (R)-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahydroisoquinoline-6- sulfonamide and S-adenosylmethionine===
-Description: SET7/9 in complex with inhibitor N-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahtdroisoquinoline-6-sulfonamide and S-adenosylmethionine

OCA: Protected "4e47" [edit=sysop:move=sysop]

2012-03-21T07:16:34Z

Protected "4e47" [edit=sysop:move=sysop]

← Older revision	Revision as of 07:16, 21 March 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4e47 is ON HOLD Authors: Walker, J.R., Ouyang, H., Dong, A., Barsyte, D., Vedadi, M., Bountra, C., Weigelt, J., Edwards, A.M., Arrowsmith, C.H., Bro...

2012-03-21T07:16:33Z

New page: '''Unreleased structure''' The entry 4e47 is ON HOLD Authors: Walker, J.R., Ouyang, H., Dong, A., Barsyte, D., Vedadi, M., Bountra, C., Weigelt, J., Edwards, A.M., Arrowsmith, C.H., Bro...

New page

'''Unreleased structure'''

The entry 4e47 is ON HOLD

Authors: Walker, J.R., Ouyang, H., Dong, A., Barsyte, D., Vedadi, M., Bountra, C., Weigelt, J., Edwards, A.M., Arrowsmith, C.H., Brown, P.J., Structural Genomics Consortium (SGC)

Description: SET7/9 in complex with inhibitor N-(3-(3-cyanophenyl)-1-oxo-1-(pyrrolidin-1-yl)propan-2-yl)-1,2,3,4-tetrahtdroisoquinoline-6-sulfonamide and S-adenosylmethionine