3vuz - Revision history

OCA at 12:38, 8 November 2023

OCA — Wed, 08 Nov 2023 12:38:23 GMT

←Older revision		Revision as of 12:38, 8 November 2023
Line 3:		Line 3:
	<StructureSection load='3vuz' size='340' side='right'caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3vuz' size='340' side='right'caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3vuz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VUZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3vuz]] is a 1 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=3VUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VUZ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=K15:5~~-{[~~(3S)-3-AMINO-3-CARBOXYPROPYL](HEXYL)AMINO}-5-DEOXYADENOSINE'>K15</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]] 2.5Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[~~[Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3vv0\|3vv0]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K15:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](HEXYL)AMINO}-5-DEOXYADENOSINE'>K15</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>SETD7, KIAA1717, KMT7, SET7, SET9 ([https://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'>[https~~:~~//en.wikipedia.org/wiki/Histone~~-~~lysine_N~~-~~methyltransferase Histone~~-~~lysine N~~-~~methyltransferase~~]~~, with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3vuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vuz OCA], [https://pdbe.org/3vuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vuz RCSB], [https://www.ebi.ac.uk/pdbsum/3vuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vuz 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=3vuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vuz OCA], [https://pdbe.org/3vuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vuz RCSB], [https://www.ebi.ac.uk/pdbsum/3vuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vuz 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histone-lysine N-methyltransferase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Handa, N]]	+	[[Category: Handa N]]
-	[[Category: Hirano, T]]	+	[[Category: Hirano T]]
-	[[Category: Honda, K]]	+	[[Category: Honda K]]
-	[[Category: Kagechika, H]]	+	[[Category: Kagechika H]]
-	[[Category: Niwa, H]]	+	[[Category: Niwa H]]
-	[[Category: Ohsawa, N]]	+	[[Category: Ohsawa N]]
-	[[Category: Shirouzu, M]]	+	[[Category: Shirouzu M]]
-	[[Category: Tomabechi, Y]]	+	[[Category: Tomabechi Y]]
-	[[Category: Toyama, M]]	+	[[Category: Toyama M]]
-	[[Category: Umehara, T]]	+	[[Category: Umehara T]]
-	[[Category: Yokoyama, S]]	+	[[Category: Yokoyama S]]
-	~~[[Category: Adenosylmethionine binding]]~~	+
-	~~[[Category: Set domain]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 19:05, 27 July 2022

OCA — Wed, 27 Jul 2022 19:05:29 GMT

←Older revision		Revision as of 19:05, 27 July 2022
Line 1:		Line 1:

	==Crystal structure of histone methyltransferase SET7/9 in complex with AAM-1==		==Crystal structure of histone methyltransferase SET7/9 in complex with AAM-1==
-	<StructureSection load='3vuz' size='340' side='right' caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='3vuz' size='340' side='right'caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3vuz]] is a 1 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=3VUZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3VUZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3vuz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VUZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K15:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](HEXYL)AMINO}-5-DEOXYADENOSINE'>K15</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K15:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](HEXYL)AMINO}-5-DEOXYADENOSINE'>K15</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vv0\|3vv0]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vv0\|3vv0]]</div></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='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SETD7, KIAA1717, KMT7, SET7, SET9 ([https://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'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://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=3vuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vuz OCA], [~~http~~://pdbe.org/3vuz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3vuz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3vuz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3vuz 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=3vuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vuz OCA], [https://pdbe.org/3vuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vuz RCSB], [https://www.ebi.ac.uk/pdbsum/3vuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vuz 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[Histone methyltransferase\|Histone methyltransferase]]	+	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Handa, N]]		[[Category: Handa, N]]
	[[Category: Hirano, T]]		[[Category: Hirano, T]]

OCA at 09:13, 3 October 2016

OCA — Mon, 03 Oct 2016 09:13:15 GMT

←Older revision		Revision as of 09:13, 3 October 2016
Line 1:		Line 1:

-	==Crystal structure of histone methyltransferase SET7/9 in ~~comlex~~ with AAM-1==	+	==Crystal structure of histone methyltransferase SET7/9 in complex with AAM-1==
	<StructureSection load='3vuz' size='340' side='right' caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3vuz' size='340' side='right' caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==

OCA at 18:40, 4 August 2016

OCA — Thu, 04 Aug 2016 18:40:07 GMT

←Older revision		Revision as of 18:40, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of histone methyltransferase SET7/9 in comlex with AAM-1==		==Crystal structure of histone methyltransferase SET7/9 in comlex with AAM-1==
	<StructureSection load='3vuz' size='340' side='right' caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3vuz' size='340' side='right' caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>
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	<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='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=3vuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vuz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vuz RCSB], [http://www.ebi.ac.uk/pdbsum/3vuz 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=3vuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vuz OCA], [http://pdbe.org/3vuz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vuz RCSB], [http://www.ebi.ac.uk/pdbsum/3vuz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vuz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 3vuz" style="background-color:#fffaf0;"></div>

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

OCA at 18:18, 24 December 2014

OCA — Wed, 24 Dec 2014 18:18:46 GMT

←Older revision		Revision as of 18:18, 24 December 2014
Line 2:		Line 2:
	<StructureSection load='3vuz' size='340' side='right' caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3vuz' size='340' side='right' caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3vuz]] is a 1 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=3VUZ OCA]. <br>	+	<table><tr><td colspan='2'>[[3vuz]] is a 1 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=3VUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VUZ FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K15:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](HEXYL)AMINO}-5-DEOXYADENOSINE'>K15</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K15:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](HEXYL)AMINO}-5-DEOXYADENOSINE'>K15</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vv0\|3vv0]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vv0\|3vv0]]</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 HUMAN])</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><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Glucokinase Glucokinase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=3vuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vuz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vuz RCSB], [http://www.ebi.ac.uk/pdbsum/3vuz 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=3vuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vuz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vuz RCSB], [http://www.ebi.ac.uk/pdbsum/3vuz 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 15:		Line 17:
	Structures of histone methyltransferase SET7/9 in complexes with adenosylmethionine derivatives.,Niwa H, Handa N, Tomabechi Y, Honda K, Toyama M, Ohsawa N, Shirouzu M, Kagechika H, Hirano T, Umehara T, Yokoyama S Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):595-602. doi:, 10.1107/S0907444912052092. Epub 2013 Mar 14. PMID:23519668<ref>PMID:23519668</ref>		Structures of histone methyltransferase SET7/9 in complexes with adenosylmethionine derivatives.,Niwa H, Handa N, Tomabechi Y, Honda K, Toyama M, Ohsawa N, Shirouzu M, Kagechika H, Hirano T, Umehara T, Yokoyama S Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):595-602. doi:, 10.1107/S0907444912052092. Epub 2013 Mar 14. PMID:23519668<ref>PMID:23519668</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
		+
		+	==See Also==
		+	*[[Histone methyltransferase\|Histone methyltransferase]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 28:
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Handa, N.]]	+	[[Category: Handa, N]]
-	[[Category: Hirano, T.]]	+	[[Category: Hirano, T]]
-	[[Category: Honda, K.]]	+	[[Category: Honda, K]]
-	[[Category: Kagechika, H.]]	+	[[Category: Kagechika, H]]
-	[[Category: Niwa, H.]]	+	[[Category: Niwa, H]]
-	[[Category: Ohsawa, N.]]	+	[[Category: Ohsawa, N]]
-	[[Category: Shirouzu, M.]]	+	[[Category: Shirouzu, M]]
-	[[Category: Tomabechi, Y.]]	+	[[Category: Tomabechi, Y]]
-	[[Category: Toyama, M.]]	+	[[Category: Toyama, M]]
-	[[Category: Umehara, T.]]	+	[[Category: Umehara, T]]
-	[[Category: Yokoyama, S.]]	+	[[Category: Yokoyama, S]]
	[[Category: Adenosylmethionine binding]]		[[Category: Adenosylmethionine binding]]
	[[Category: Set domain]]		[[Category: Set domain]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Transferase-transferase inhibitor complex]]		[[Category: Transferase-transferase inhibitor complex]]

OCA at 09:34, 1 May 2014

OCA — Thu, 01 May 2014 09:34:48 GMT

←Older revision		Revision as of 09:34, 1 May 2014
Line 2:		Line 2:
	<StructureSection load='3vuz' size='340' side='right' caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='3vuz' size='340' side='right' caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	[[3vuz]] is a 1 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=3VUZ OCA]. <br>	+	<table><tr><td colspan='2'>[[3vuz]] is a 1 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=3VUZ OCA]. <br>
-	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=K15:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](HEXYL)AMINO}-5-DEOXYADENOSINE'>K15</scene><br>	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K15:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](HEXYL)AMINO}-5-DEOXYADENOSINE'>K15</scene><br>
-	<b>[[Related_structure\|Related:]]</b> [[3vv0\|3vv0]]<br>	+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3vv0\|3vv0]]</td></tr>
-	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><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 HUMAN])</td></tr>
-	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vuz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vuz RCSB], [http://www.ebi.ac.uk/pdbsum/3vuz PDBsum]</span><br>	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=3vuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vuz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vuz RCSB], [http://www.ebi.ac.uk/pdbsum/3vuz PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	SET7/9 is a protein lysine methyltransferase that methylates histone H3 and nonhistone proteins such as p53, TAF10 and oestrogen receptor alpha. In previous work, novel inhibitors of SET7/9 that are amine analogues of the coenzyme S-(5'-adenosyl)-L-methionine (AdoMet) have been developed. Here, crystal structures of SET7/9 are reported in complexes with two AdoMet analogues, designated DAAM-3 and AAM-1, in which an n-hexylaminoethyl group or an n-hexyl group is attached to the N atom that replaces the S atom of AdoMet, respectively. In both structures, the inhibitors bind to the coenzyme-binding site and their additional alkyl chain binds in the lysine-access channel. The N atom in the azaalkyl chain of DAAM-3 is located at almost the same position as the N-methyl C atom of the methylated lysine side chain in the substrate-peptide complex structures and stabilizes complex formation by hydrogen bonding to the substrate-binding site residues of SET7/9. On the other hand, the alkyl chain of AAM-1, which is a weaker inhibitor than DAAM-3, binds in the lysine-access channel only through hydrophobic and van der Waals interactions. Unexpectedly, the substrate-binding site of SET7/9 complexed with AAM-1 specifically interacts with the artificial N-terminal sequence of an adjacent symmetry-related molecule, presumably stabilizing the alkyl chain of AAM-1.		SET7/9 is a protein lysine methyltransferase that methylates histone H3 and nonhistone proteins such as p53, TAF10 and oestrogen receptor alpha. In previous work, novel inhibitors of SET7/9 that are amine analogues of the coenzyme S-(5'-adenosyl)-L-methionine (AdoMet) have been developed. Here, crystal structures of SET7/9 are reported in complexes with two AdoMet analogues, designated DAAM-3 and AAM-1, in which an n-hexylaminoethyl group or an n-hexyl group is attached to the N atom that replaces the S atom of AdoMet, respectively. In both structures, the inhibitors bind to the coenzyme-binding site and their additional alkyl chain binds in the lysine-access channel. The N atom in the azaalkyl chain of DAAM-3 is located at almost the same position as the N-methyl C atom of the methylated lysine side chain in the substrate-peptide complex structures and stabilizes complex formation by hydrogen bonding to the substrate-binding site residues of SET7/9. On the other hand, the alkyl chain of AAM-1, which is a weaker inhibitor than DAAM-3, binds in the lysine-access channel only through hydrophobic and van der Waals interactions. Unexpectedly, the substrate-binding site of SET7/9 complexed with AAM-1 specifically interacts with the artificial N-terminal sequence of an adjacent symmetry-related molecule, presumably stabilizing the alkyl chain of AAM-1.
Line 13:		Line 16:

	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:09, 30 April 2014

OCA — Wed, 30 Apr 2014 10:09:44 GMT

←Older revision		Revision as of 10:09, 30 April 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	[[3vuz]] is a 1 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=3VUZ OCA]. <br>		[[3vuz]] is a 1 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=3VUZ OCA]. <br>
-	<b>Related:</b> [[3vv0\|3vv0]]<br>	+	<b>[[Ligand\|Ligands:]]</b> <scene name='pdbligand=K15:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](HEXYL)AMINO}-5-DEOXYADENOSINE'>K15</scene><br>
		+	<b>[[Related_structure\|Related:]]</b> [[3vv0\|3vv0]]<br>
	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>		<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vuz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vuz RCSB], [http://www.ebi.ac.uk/pdbsum/3vuz PDBsum]</span><br>
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	SET7/9 is a protein lysine methyltransferase that methylates histone H3 and nonhistone proteins such as p53, TAF10 and oestrogen receptor alpha. In previous work, novel inhibitors of SET7/9 that are amine analogues of the coenzyme S-(5'-adenosyl)-L-methionine (AdoMet) have been developed. Here, crystal structures of SET7/9 are reported in complexes with two AdoMet analogues, designated DAAM-3 and AAM-1, in which an n-hexylaminoethyl group or an n-hexyl group is attached to the N atom that replaces the S atom of AdoMet, respectively. In both structures, the inhibitors bind to the coenzyme-binding site and their additional alkyl chain binds in the lysine-access channel. The N atom in the azaalkyl chain of DAAM-3 is located at almost the same position as the N-methyl C atom of the methylated lysine side chain in the substrate-peptide complex structures and stabilizes complex formation by hydrogen bonding to the substrate-binding site residues of SET7/9. On the other hand, the alkyl chain of AAM-1, which is a weaker inhibitor than DAAM-3, binds in the lysine-access channel only through hydrophobic and van der Waals interactions. Unexpectedly, the substrate-binding site of SET7/9 complexed with AAM-1 specifically interacts with the artificial N-terminal sequence of an adjacent symmetry-related molecule, presumably stabilizing the alkyl chain of AAM-1.		SET7/9 is a protein lysine methyltransferase that methylates histone H3 and nonhistone proteins such as p53, TAF10 and oestrogen receptor alpha. In previous work, novel inhibitors of SET7/9 that are amine analogues of the coenzyme S-(5'-adenosyl)-L-methionine (AdoMet) have been developed. Here, crystal structures of SET7/9 are reported in complexes with two AdoMet analogues, designated DAAM-3 and AAM-1, in which an n-hexylaminoethyl group or an n-hexyl group is attached to the N atom that replaces the S atom of AdoMet, respectively. In both structures, the inhibitors bind to the coenzyme-binding site and their additional alkyl chain binds in the lysine-access channel. The N atom in the azaalkyl chain of DAAM-3 is located at almost the same position as the N-methyl C atom of the methylated lysine side chain in the substrate-peptide complex structures and stabilizes complex formation by hydrogen bonding to the substrate-binding site residues of SET7/9. On the other hand, the alkyl chain of AAM-1, which is a weaker inhibitor than DAAM-3, binds in the lysine-access channel only through hydrophobic and van der Waals interactions. Unexpectedly, the substrate-binding site of SET7/9 complexed with AAM-1 specifically interacts with the artificial N-terminal sequence of an adjacent symmetry-related molecule, presumably stabilizing the alkyl chain of AAM-1.

OCA at 05:22, 30 April 2014

OCA — Wed, 30 Apr 2014 05:22:46 GMT

←Older revision		Revision as of 05:22, 30 April 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3vuz\| PDB=3vuz \| SCENE= }}~~	+	==Crystal structure of histone methyltransferase SET7/9 in comlex with AAM-1==
-	===Crystal structure of histone methyltransferase SET7/9 in comlex with AAM-1===	+	<StructureSection load='3vuz' size='340' side='right' caption='[[3vuz]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	[[3vuz]] is a 1 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=3VUZ OCA]. <br>
		+	<b>Related:</b> [[3vv0\|3vv0]]<br>
		+	<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
		+	== Publication Abstract from PubMed ==
		+	SET7/9 is a protein lysine methyltransferase that methylates histone H3 and nonhistone proteins such as p53, TAF10 and oestrogen receptor alpha. In previous work, novel inhibitors of SET7/9 that are amine analogues of the coenzyme S-(5'-adenosyl)-L-methionine (AdoMet) have been developed. Here, crystal structures of SET7/9 are reported in complexes with two AdoMet analogues, designated DAAM-3 and AAM-1, in which an n-hexylaminoethyl group or an n-hexyl group is attached to the N atom that replaces the S atom of AdoMet, respectively. In both structures, the inhibitors bind to the coenzyme-binding site and their additional alkyl chain binds in the lysine-access channel. The N atom in the azaalkyl chain of DAAM-3 is located at almost the same position as the N-methyl C atom of the methylated lysine side chain in the substrate-peptide complex structures and stabilizes complex formation by hydrogen bonding to the substrate-binding site residues of SET7/9. On the other hand, the alkyl chain of AAM-1, which is a weaker inhibitor than DAAM-3, binds in the lysine-access channel only through hydrophobic and van der Waals interactions. Unexpectedly, the substrate-binding site of SET7/9 complexed with AAM-1 specifically interacts with the artificial N-terminal sequence of an adjacent symmetry-related molecule, presumably stabilizing the alkyl chain of AAM-1.

-	~~==Function==~~	+	Structures of histone methyltransferase SET7/9 in complexes with adenosylmethionine derivatives.,Niwa H, Handa N, Tomabechi Y, Honda K, Toyama M, Ohsawa N, Shirouzu M, Kagechika H, Hirano T, Umehara T, Yokoyama S Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):595-602. doi:, 10.1107/S0907444912052092. Epub 2013 Mar 14. PMID:23519668<ref>PMID:23519668</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>	+

-	~~==About this Structure==~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3vuz]] is~~ a ~~1 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=3VUZ OCA]~~.	+	== References ==
-		+	<references/>
-	==~~Reference~~==	+	__TOC__
-	<references ~~group="xtra"~~/><~~references~~/>	+	</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Handa, N.]]		[[Category: Handa, N.]]
	[[Category: Hirano, T.]]		[[Category: Hirano, T.]]

OCA at 08:53, 27 March 2013

OCA — Wed, 27 Mar 2013 08:53:09 GMT

←Older revision		Revision as of 08:53, 27 March 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_3vuz\| PDB=3vuz \| SCENE= }}
		+	===Crystal structure of histone methyltransferase SET7/9 in comlex with AAM-1===

-	~~The entry 3vuz is ON HOLD until Paper Publication~~	+	==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>

-	~~Authors~~: ~~Niwa, H~~.~~, Handa, N~~.~~, Tomabechi, Y~~.~~, Honda, K., Toyama, M., Ohsawa, N., Shirouzu, M., Kagechika, H~~.~~, Hirano, T~~.~~, Umehara, T~~.~~, Yokoyama, S~~.	+	==About this Structure==
		+	[[3vuz]] is a 1 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=3VUZ OCA].

-	~~Description~~:	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Histone-lysine N-methyltransferase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Handa, N.]]
		+	[[Category: Hirano, T.]]
		+	[[Category: Honda, K.]]
		+	[[Category: Kagechika, H.]]
		+	[[Category: Niwa, H.]]
		+	[[Category: Ohsawa, N.]]
		+	[[Category: Shirouzu, M.]]
		+	[[Category: Tomabechi, Y.]]
		+	[[Category: Toyama, M.]]
		+	[[Category: Umehara, T.]]
		+	[[Category: Yokoyama, S.]]
		+	[[Category: Adenosylmethionine binding]]
		+	[[Category: Set domain]]
		+	[[Category: Transferase]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 05:08, 15 August 2012

OCA — Wed, 15 Aug 2012 05:08:51 GMT

←Older revision		Revision as of 05:08, 15 August 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3vuz is ON HOLD	+	The entry 3vuz is ON HOLD until Paper Publication

	Authors: Niwa, H., Handa, N., Tomabechi, Y., Honda, K., Toyama, M., Ohsawa, N., Shirouzu, M., Kagechika, H., Hirano, T., Umehara, T., Yokoyama, S.		Authors: Niwa, H., Handa, N., Tomabechi, Y., Honda, K., Toyama, M., Ohsawa, N., Shirouzu, M., Kagechika, H., Hirano, T., Umehara, T., Yokoyama, S.

	Description:		Description: