4x8p - Revision history

OCA at 13:00, 1 March 2024

OCA — Fri, 01 Mar 2024 13:00:14 GMT

←Older revision		Revision as of 13:00, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4x8p]] is a 2 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=4X8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X8P FirstGlance]. <br>		<table><tr><td colspan='2'>[[4x8p]] is a 2 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=4X8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X8P FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4x8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8p OCA], [https://pdbe.org/4x8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x8p RCSB], [https://www.ebi.ac.uk/pdbsum/4x8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x8p 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=4x8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8p OCA], [https://pdbe.org/4x8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x8p RCSB], [https://www.ebi.ac.uk/pdbsum/4x8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x8p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/ASH2L_HUMAN ASH2L_HUMAN] Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.<ref>PMID:12670868</ref> <ref>PMID:19556245</ref>		[https://www.uniprot.org/uniprot/ASH2L_HUMAN ASH2L_HUMAN] Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.<ref>PMID:12670868</ref> <ref>PMID:19556245</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The methyltransferase activity of the trithorax group (TrxG) protein MLL1 found within its COMPASS (complex associated with SET1)-like complex is allosterically regulated by a four-subunit complex composed of WDR5, RbBP5, Ash2L, and DPY30 (also referred to as WRAD). We report structural evidence showing that in WRAD, a concave surface of the Ash2L SPIa and ryanodine receptor (SPRY) domain binds to a cluster of acidic residues, referred to as the D/E box, in RbBP5. Mutational analysis shows that residues forming the Ash2L/RbBP5 interface are important for heterodimer formation, stimulation of MLL1 catalytic activity, and erythroid cell terminal differentiation. We also demonstrate that a phosphorylation switch on RbBP5 stimulates WRAD complex formation and significantly increases KMT2 (lysine [K] methyltransferase 2) enzyme methylation rates. Overall, our findings provide structural insights into the assembly of the WRAD complex and point to a novel regulatory mechanism controlling the activity of the KMT2/COMPASS family of lysine methyltransferases.
-
-	A phosphorylation switch on RbBP5 regulates histone H3 Lys4 methylation.,Zhang P, Chaturvedi CP, Tremblay V, Cramet M, Brunzelle JS, Skiniotis G, Brand M, Shilatifard A, Couture JF Genes Dev. 2015 Jan 15;29(2):123-8. doi: 10.1101/gad.254870.114. PMID:25593305<ref>PMID:25593305</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4x8p" style="background-color:#fffaf0;"></div>

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

OCA at 21:18, 12 April 2023

OCA — Wed, 12 Apr 2023 21:18:07 GMT

←Older revision		Revision as of 21:18, 12 April 2023
Line 3:		Line 3:
	<StructureSection load='4x8p' size='340' side='right'caption='[[4x8p]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='4x8p' size='340' side='right'caption='[[4x8p]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4x8p]] is a 2 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=4X8P OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4X8P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4x8p]] is a 2 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=4X8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X8P FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4x8n\|4x8n]]</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=4x8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8p OCA], [https://pdbe.org/4x8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x8p RCSB], [https://www.ebi.ac.uk/pdbsum/4x8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x8p ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ASH2L, ASH2L1 ([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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4x8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8p OCA], [~~http~~://pdbe.org/4x8p PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4x8p RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4x8p PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4x8p ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ASH2L_HUMAN ASH2L_HUMAN]] Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.<ref>PMID:12670868</ref> <ref>PMID:19556245</ref> [[http://www.uniprot.org/uniprot/RBBP5_HUMAN RBBP5_HUMAN]] In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation.<ref>PMID:19556245</ref>	+	[https://www.uniprot.org/uniprot/ASH2L_HUMAN ASH2L_HUMAN] Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.<ref>PMID:12670868</ref> <ref>PMID:19556245</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
-	*[[Histone methyltransferase\|Histone methyltransferase]]	+	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Brand, M]]	+	[[Category: Brand M]]
-	[[Category: Brunzelle~~, J S~~]]	+	[[Category: Brunzelle JS]]
-	[[Category: Chaturvedi~~, C P~~]]	+	[[Category: Chaturvedi CP]]
-	[[Category: Couture, J F]]	+	[[Category: Couture J-F]]
-	[[Category: Shilatifard, A]]	+	[[Category: Shilatifard A]]
-	[[Category: Skiniotis, G]]	+	[[Category: Skiniotis G]]
-	[[Category: Zhang, P]]	+	[[Category: Zhang P]]
-	~~[[Category: Epigenetic]]~~	+
-	~~[[Category: Histone]]~~	+
-	~~[[Category: Mll1]]~~	+
-	~~[[Category: Protein binding~~]]	+

OCA at 07:24, 29 May 2019

OCA — Wed, 29 May 2019 07:24:03 GMT

←Older revision		Revision as of 07:24, 29 May 2019
Line 1:		Line 1:

	==Crystal structure of Ash2L SPRY domain in complex with RbBP5==		==Crystal structure of Ash2L SPRY domain in complex with RbBP5==
-	<StructureSection load='4x8p' size='340' side='right' caption='[[4x8p]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='4x8p' size='340' side='right'caption='[[4x8p]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4x8p]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X8P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4x8p]] is a 2 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=4X8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X8P FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4x8n\|4x8n]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4x8n\|4x8n]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ASH2L, ASH2L1 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8p OCA], [http://pdbe.org/4x8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x8p RCSB], [http://www.ebi.ac.uk/pdbsum/4x8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x8p ProSAT]</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=4x8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8p OCA], [http://pdbe.org/4x8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x8p RCSB], [http://www.ebi.ac.uk/pdbsum/4x8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x8p ProSAT]</span></td></tr>
	</table>		</table>
Line 19:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4x8p" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4x8p" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone methyltransferase\|Histone methyltransferase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Brand, M]]		[[Category: Brand, M]]
	[[Category: Brunzelle, J S]]		[[Category: Brunzelle, J S]]

OCA at 12:56, 11 August 2016

OCA — Thu, 11 Aug 2016 12:56:36 GMT

←Older revision		Revision as of 12:56, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Ash2L SPRY domain in complex with RbBP5==		==Crystal structure of Ash2L SPRY domain in complex with RbBP5==
	<StructureSection load='4x8p' size='340' side='right' caption='[[4x8p]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='4x8p' size='340' side='right' caption='[[4x8p]], [[Resolution\|resolution]] 2.20Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4x8n\|4x8n]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4x8n\|4x8n]]</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=4x8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x8p RCSB], [http://www.ebi.ac.uk/pdbsum/4x8p 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=4x8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8p OCA], [http://pdbe.org/4x8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x8p RCSB], [http://www.ebi.ac.uk/pdbsum/4x8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x8p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4x8p" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:37, 28 January 2015

OCA — Wed, 28 Jan 2015 16:37:05 GMT

←Older revision		Revision as of 16:37, 28 January 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of Ash2L SPRY domain in complex with RbBP5==
		+	<StructureSection load='4x8p' size='340' side='right' caption='[[4x8p]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4x8p]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X8P FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4x8n\|4x8n]]</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=4x8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x8p RCSB], [http://www.ebi.ac.uk/pdbsum/4x8p PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ASH2L_HUMAN ASH2L_HUMAN]] Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.<ref>PMID:12670868</ref> <ref>PMID:19556245</ref> [[http://www.uniprot.org/uniprot/RBBP5_HUMAN RBBP5_HUMAN]] In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation.<ref>PMID:19556245</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The methyltransferase activity of the trithorax group (TrxG) protein MLL1 found within its COMPASS (complex associated with SET1)-like complex is allosterically regulated by a four-subunit complex composed of WDR5, RbBP5, Ash2L, and DPY30 (also referred to as WRAD). We report structural evidence showing that in WRAD, a concave surface of the Ash2L SPIa and ryanodine receptor (SPRY) domain binds to a cluster of acidic residues, referred to as the D/E box, in RbBP5. Mutational analysis shows that residues forming the Ash2L/RbBP5 interface are important for heterodimer formation, stimulation of MLL1 catalytic activity, and erythroid cell terminal differentiation. We also demonstrate that a phosphorylation switch on RbBP5 stimulates WRAD complex formation and significantly increases KMT2 (lysine [K] methyltransferase 2) enzyme methylation rates. Overall, our findings provide structural insights into the assembly of the WRAD complex and point to a novel regulatory mechanism controlling the activity of the KMT2/COMPASS family of lysine methyltransferases.

-	~~The entry 4x8p is ON HOLD until Paper Publication~~	+	A phosphorylation switch on RbBP5 regulates histone H3 Lys4 methylation.,Zhang P, Chaturvedi CP, Tremblay V, Cramet M, Brunzelle JS, Skiniotis G, Brand M, Shilatifard A, Couture JF Genes Dev. 2015 Jan 15;29(2):123-8. doi: 10.1101/gad.254870.114. PMID:25593305<ref>PMID:25593305</ref>

-	~~Authors: Zhang~~, ~~P., Chaturvedi, C.P., Brunzelle, J~~.S.~~, Skiniotis, G., Brand, M., Shilatifard, A., Couture, J.-F~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Crystal structure of Ash2L SPRY domain in complex with RbBP5~~	+	== References ==
-	~~[[Category: Unreleased Structures]]~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Brand, M]]		[[Category: Brand, M]]
-	[[Category: Couture, J.-F]]	+	[[Category: Brunzelle, J S]]
		+	[[Category: Chaturvedi, C P]]
		+	[[Category: Couture, J F]]
	[[Category: Shilatifard, A]]		[[Category: Shilatifard, A]]
	[[Category: Skiniotis, G]]		[[Category: Skiniotis, G]]
-	[[Category: Chaturvedi, C.P]]
	[[Category: Zhang, P]]		[[Category: Zhang, P]]
-	[[Category: ~~Brunzelle, J.S~~]]	+	[[Category: Epigenetic]]
		+	[[Category: Histone]]
		+	[[Category: Mll1]]
		+	[[Category: Protein binding]]

OCA at 15:38, 21 January 2015

OCA — Wed, 21 Jan 2015 15:38:40 GMT

←Older revision		Revision as of 15:38, 21 January 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4x8p is ON HOLD	+	The entry 4x8p is ON HOLD until Paper Publication

-	Authors: Zhang P, Chaturvedi CP, Brunzelle JS, Skiniotis G, Brand M, Shilatifard A, Couture J-F	+	Authors: Zhang, P., Chaturvedi, C.P., Brunzelle, J.S., Skiniotis, G., Brand, M., Shilatifard, A., Couture, J.-F.

	Description: Crystal structure of Ash2L SPRY domain in complex with RbBP5		Description: Crystal structure of Ash2L SPRY domain in complex with RbBP5
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: ~~Zhang P~~, ~~Chaturvedi Cp~~, ~~Brunzelle Js~~, Skiniotis G, ~~Brand M~~, ~~Shilatifard A~~, ~~Couture~~ J-F]]	+	[[Category: Brand, M]]
		+	[[Category: Couture, J.-F]]
		+	[[Category: Shilatifard, A]]
		+	[[Category: Skiniotis, G]]
		+	[[Category: Chaturvedi, C.P]]
		+	[[Category: Zhang, P]]
		+	[[Category: Brunzelle, J.S]]

OCA at 20:39, 24 December 2014

OCA — Wed, 24 Dec 2014 20:39:50 GMT

←Older revision		Revision as of 20:39, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of Ash2L SPRY domain in complex with RbBP5		Description: Crystal structure of Ash2L SPRY domain in complex with RbBP5
		+	[[Category: Unreleased Structures]]
		+	[[Category: Zhang P, Chaturvedi Cp, Brunzelle Js, Skiniotis G, Brand M, Shilatifard A, Couture J-F]]

OCA: Protected "4x8p" [edit=sysop:move=sysop]

OCA — Wed, 17 Dec 2014 11:47:34 GMT

Protected "4x8p" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:47, 17 December 2014

OCA: New page: '''Unreleased structure''' The entry 4x8p is ON HOLD Authors: Zhang P, Chaturvedi CP, Brunzelle JS, Skiniotis G, Brand M, Shilatifard A, Couture J-F Description: Crystal structure of A...

OCA — Wed, 17 Dec 2014 11:47:33 GMT

New page: '''Unreleased structure''' The entry 4x8p is ON HOLD Authors: Zhang P, Chaturvedi CP, Brunzelle JS, Skiniotis G, Brand M, Shilatifard A, Couture J-F Description: Crystal structure of A...

New page

'''Unreleased structure'''

The entry 4x8p is ON HOLD

Authors: Zhang P, Chaturvedi CP, Brunzelle JS, Skiniotis G, Brand M, Shilatifard A, Couture J-F

Description: Crystal structure of Ash2L SPRY domain in complex with RbBP5