5h25 - Revision history

OCA at 07:21, 9 August 2023

OCA — Wed, 09 Aug 2023 07:21:28 GMT

←Older revision		Revision as of 07:21, 9 August 2023
Line 3:		Line 3:
	<StructureSection load='5h25' size='340' side='right'caption='[[5h25]], [[Resolution\|resolution]] 2.88Å' scene=''>		<StructureSection load='5h25' size='340' side='right'caption='[[5h25]], [[Resolution\|resolution]] 2.88Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5h25]] 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=5H25 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5H25 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5h25]] 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=5H25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H25 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=LQH:5~~-~~(2-FLUOROPHENYL)-2~~,~~3-DIHYDROIMIDAZO~~[~~2,1-A]ISOQUINOLINE'>LQH</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]] 2.88Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[~~[Related_structure~~\|~~Related:]]</b></td><td class="sblockDat">[[5h13\|5h13]], [[5h14\|5h14]], [[5h15\|5h15]], [[5h17\|5h17]], [[5h19\|5h19]], [[5h24\|5h24~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LQH:5-(2-FLUOROPHENYL)-2,3-DIHYDROIMIDAZO[2,1-A]ISOQUINOLINE'>LQH</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>EED ([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=5h25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h25 OCA], [https://pdbe.org/5h25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h25 RCSB], [https://www.ebi.ac.uk/pdbsum/5h25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h25 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~~://proteopedia.org/fgij/fg.htm?mol=5h25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h25 OCA], [~~http~~://pdbe.org/5h25 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5h25 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5h25 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5h25 ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Disease ==
-	[[http://www.uniprot.org/uniprot/EZH2_HUMAN EZH2_HUMAN]] Weaver syndrome. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/EED_HUMAN EED_HUMAN]] Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A.<ref>PMID:9584199</ref> <ref>PMID:10581039</ref> <ref>PMID:14532106</ref> <ref>PMID:15385962</ref> <ref>PMID:15231737</ref> <ref>PMID:15225548</ref> <ref>PMID:16357870</ref> <ref>PMID:18285464</ref> <ref>PMID:20974918</ref> [[http://www.uniprot.org/uniprot/EZH2_HUMAN EZH2_HUMAN]] Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Compared to EZH2-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA.<ref>PMID:14532106</ref> <ref>PMID:15385962</ref> <ref>PMID:15231737</ref> <ref>PMID:15225548</ref> <ref>PMID:16179254</ref> <ref>PMID:16618801</ref> <ref>PMID:16357870</ref> <ref>PMID:16936726</ref> <ref>PMID:17210787</ref> <ref>PMID:17344414</ref> <ref>PMID:19026781</ref> <ref>PMID:18285464</ref> <ref>PMID:20935635</ref> <ref>PMID:23063525</ref>	+	[https://www.uniprot.org/uniprot/EED_HUMAN EED_HUMAN] Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A.<ref>PMID:9584199</ref> <ref>PMID:10581039</ref> <ref>PMID:14532106</ref> <ref>PMID:15385962</ref> <ref>PMID:15231737</ref> <ref>PMID:15225548</ref> <ref>PMID:16357870</ref> <ref>PMID:18285464</ref> <ref>PMID:20974918</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 21:

	==See Also==		==See Also==
-	*[[Polycomb\|Polycomb]]	+	*[[Polycomb complex proteins 3D structures\|Polycomb complex proteins 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histone-lysine N-methyltransferase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Luo, X]]	+	[[Category: Luo X]]
-	[[Category: Zhang, H]]	+	[[Category: Zhang H]]
-	[[Category: Zhao, K]]	+	[[Category: Zhao K]]
-	[[Category: Zhao, M]]	+	[[Category: Zhao M]]
-	~~[[Category: Eed]]~~	+
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Prc2]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 06:50, 20 May 2020

OCA — Wed, 20 May 2020 06:50:07 GMT

←Older revision		Revision as of 06:50, 20 May 2020
Line 1:		Line 1:

	==EED in complex with PRC2 allosteric inhibitor compound 11==		==EED in complex with PRC2 allosteric inhibitor compound 11==
-	<StructureSection load='5h25' size='340' side='right' caption='[[5h25]], [[Resolution\|resolution]] 2.88Å' scene=''>	+	<StructureSection load='5h25' size='340' side='right'caption='[[5h25]], [[Resolution\|resolution]] 2.88Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5h25]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H25 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5H25 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5h25]] 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=5H25 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H25 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LQH:5-(2-FLUOROPHENYL)-2,3-DIHYDROIMIDAZO[2,1-A]ISOQUINOLINE'>LQH</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LQH:5-(2-FLUOROPHENYL)-2,3-DIHYDROIMIDAZO[2,1-A]ISOQUINOLINE'>LQH</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h13\|5h13]], [[5h14\|5h14]], [[5h15\|5h15]], [[5h17\|5h17]], [[5h19\|5h19]], [[5h24\|5h24]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h13\|5h13]], [[5h14\|5h14]], [[5h15\|5h15]], [[5h17\|5h17]], [[5h19\|5h19]], [[5h24\|5h24]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EED ([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=5h25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h25 OCA], [http://pdbe.org/5h25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h25 RCSB], [http://www.ebi.ac.uk/pdbsum/5h25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h25 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5h25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h25 OCA], [http://pdbe.org/5h25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h25 RCSB], [http://www.ebi.ac.uk/pdbsum/5h25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h25 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 22:		Line 23:
	</div>		</div>
	<div class="pdbe-citations 5h25" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5h25" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Polycomb\|Polycomb]]
	== References ==		== References ==
	<references/>		<references/>
Line 27:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Luo, X]]		[[Category: Luo, X]]
	[[Category: Zhang, H]]		[[Category: Zhang, H]]

OCA at 23:26, 25 January 2017

OCA — Wed, 25 Jan 2017 23:26:37 GMT

←Older revision		Revision as of 23:26, 25 January 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The entry ~~5h25~~ is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==EED in complex with PRC2 allosteric inhibitor compound 11==
		+	<StructureSection load='5h25' size='340' side='right' caption='[[5h25]], [[Resolution\|resolution]] 2.88Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5h25]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H25 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H25 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LQH:5-(2-FLUOROPHENYL)-2,3-DIHYDROIMIDAZO[2,1-A]ISOQUINOLINE'>LQH</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h13\|5h13]], [[5h14\|5h14]], [[5h15\|5h15]], [[5h17\|5h17]], [[5h19\|5h19]], [[5h24\|5h24]]</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=5h25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h25 OCA], [http://pdbe.org/5h25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h25 RCSB], [http://www.ebi.ac.uk/pdbsum/5h25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h25 ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/EZH2_HUMAN EZH2_HUMAN]] Weaver syndrome. The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/EED_HUMAN EED_HUMAN]] Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A.<ref>PMID:9584199</ref> <ref>PMID:10581039</ref> <ref>PMID:14532106</ref> <ref>PMID:15385962</ref> <ref>PMID:15231737</ref> <ref>PMID:15225548</ref> <ref>PMID:16357870</ref> <ref>PMID:18285464</ref> <ref>PMID:20974918</ref> [[http://www.uniprot.org/uniprot/EZH2_HUMAN EZH2_HUMAN]] Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Compared to EZH2-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA.<ref>PMID:14532106</ref> <ref>PMID:15385962</ref> <ref>PMID:15231737</ref> <ref>PMID:15225548</ref> <ref>PMID:16179254</ref> <ref>PMID:16618801</ref> <ref>PMID:16357870</ref> <ref>PMID:16936726</ref> <ref>PMID:17210787</ref> <ref>PMID:17344414</ref> <ref>PMID:19026781</ref> <ref>PMID:18285464</ref> <ref>PMID:20935635</ref> <ref>PMID:23063525</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Overexpression and somatic heterozygous mutations of EZH2, the catalytic subunit Polycomb repressive complex 2 (PRC2), are associated with several tumor types. EZH2 inhibitor, EPZ-6438 (Tazemetostat), demonstrated clinical efficacy in patients with acceptable safety profile as monotherapy. EED, another subunit of PRC2 complex, is essential for its histone methyltransferase activity through direct binding to trimethylated lysine 27 on histone 3 (H3K27Me3). Herein we disclose the discovery of a first-in-class potent, selective and orally bioavailable EED inhibitor EED226 (compound 43). Guided by X-ray crystallography, compound 43 discovered by fragmentation and regrowth of Compound 7, a PRC2 HTS hit that directly binds EED. Scaffold hopping followed by ensuing multi-parameter optimization led to the discovery compound 43. Compound 43 induces robust and sustained tumor regression in EZH2MUT pre-clinical DLBCL model. For the first time we demonstrate that specific and direct inhibition of EED can be effective as an anti-cancer strategy.

-	~~Authors~~:	+	Discovery of First-in-Class, Potent and Orally Bioavailable EED inhibitor with Robust Anti-cancer Efficacy.,Huang Y, Zhang J, Yu Z, Zhang H, Wang Y, Lingel A, Qi W, Gu XJ, Zhao K, Shultz MD, Wang L, Fu X, Sun Y, Zhang Q, Jiang X, Zhang JW, Zhang C, Li L, Zeng J, Feng L, Zhang C, Liu Y, Zhang M, Zhang L, Zhao M, Gao Z, Liu X, Fang D, Guo H, Mi Y, Gabriel T, Dillon MP, Atadja P, Oyang C J Med Chem. 2017 Jan 16. doi: 10.1021/acs.jmedchem.6b01576. PMID:28092155<ref>PMID:28092155</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5h25" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Histone-lysine N-methyltransferase]]
		+	[[Category: Luo, X]]
		+	[[Category: Zhang, H]]
		+	[[Category: Zhao, K]]
		+	[[Category: Zhao, M]]
		+	[[Category: Eed]]
		+	[[Category: Inhibitor]]
		+	[[Category: Prc2]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 13:14, 26 October 2016

OCA — Wed, 26 Oct 2016 13:14:34 GMT

←Older revision		Revision as of 13:14, 26 October 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5h25 is ON HOLD	+	The entry 5h25 is ON HOLD until Paper Publication

-	Authors: ~~Zhao, K., Zhao, M., Luo, X., Zhang, H.~~	+	Authors:

-	Description: ~~EED in complex with an allosteric PRC2 inhibitor~~	+	Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Zhang, H]]
-	[[Category: Zhao, M]]
-	[[Category: Luo, X]]
-	[[Category: Zhao, K]]

OCA: Protected "5h25" [edit=sysop:move=sysop]

OCA — Wed, 19 Oct 2016 12:04:02 GMT

Protected "5h25" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:04, 19 October 2016

OCA: New page: '''Unreleased structure''' The entry 5h25 is ON HOLD Authors: Zhao, K., Zhao, M., Luo, X., Zhang, H. Description: EED in complex with an allosteric PRC2 inhibitor [[Category: Unrelease...

OCA — Wed, 19 Oct 2016 12:04:01 GMT

New page: '''Unreleased structure''' The entry 5h25 is ON HOLD Authors: Zhao, K., Zhao, M., Luo, X., Zhang, H. Description: EED in complex with an allosteric PRC2 inhibitor [[Category: Unrelease...

New page

'''Unreleased structure'''

The entry 5h25 is ON HOLD

Authors: Zhao, K., Zhao, M., Luo, X., Zhang, H.

Description: EED in complex with an allosteric PRC2 inhibitor
[[Category: Unreleased Structures]]
[[Category: Zhang, H]]
[[Category: Zhao, M]]
[[Category: Luo, X]]
[[Category: Zhao, K]]