6e2h - Revision history

OCA at 06:17, 11 October 2023

2023-10-11T06:17:42Z

←Older revision		Revision as of 06:17, 11 October 2023
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	<StructureSection load='6e2h' size='340' side='right'caption='[[6e2h]], [[Resolution\|resolution]] 2.24Å' scene=''>		<StructureSection load='6e2h' size='340' side='right'caption='[[6e2h]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6e2h]] is a 3 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=6E2H OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6E2H FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6e2h]] is a 3 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=6E2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E2H FirstGlance]. <br>
-	</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~~]~~), DPY30 ([http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</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]] 2.236Å</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=6e2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2h OCA], [~~http~~://pdbe.org/6e2h PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6e2h RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6e2h PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2h 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=6e2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2h OCA], [https://pdbe.org/6e2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e2h RCSB], [https://www.ebi.ac.uk/pdbsum/6e2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2h 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/DPY30_HUMAN DPY30_HUMAN]] As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.<ref>PMID:19556245</ref> <ref>PMID:19651892</ref> <ref>PMID:21335234</ref>	+	[https://www.uniprot.org/uniprot/DPY30_HUMAN DPY30_HUMAN] As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.<ref>PMID:19556245</ref> <ref>PMID:19651892</ref> <ref>PMID:21335234</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: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Brunzelle~~, J S~~]]	+	[[Category: Brunzelle JS]]
-	[[Category: Couture~~, J F~~]]	+	[[Category: Couture JF]]
-	[[Category: Joshi, M]]	+	[[Category: Joshi M]]
-	~~[[Category: Epigenetic]]~~	+
-	~~[[Category: Histone]]~~	+
-	~~[[Category: Lysine methylation]]~~	+
-	~~[[Category: Mll]]~~	+
-	~~[[Category: Nucleosome]]~~	+
-	~~[[Category: Protein binding]]~~	+
-	~~[[Category: Set1~~]]	+

OCA at 08:56, 8 January 2020

2020-01-08T08:56:53Z

←Older revision		Revision as of 08:56, 8 January 2020
Line 1:		Line 1:

	==Crystal structure of human Ash2L (SPRY domain and SDI motif) in complex with full length DPY-30==		==Crystal structure of human Ash2L (SPRY domain and SDI motif) in complex with full length DPY-30==
-	<StructureSection load='6e2h' size='340' side='right' caption='[[6e2h]], [[Resolution\|resolution]] 2.24Å' scene=''>	+	<StructureSection load='6e2h' size='340' side='right'caption='[[6e2h]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6e2h]] is a 3 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=6E2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2H FirstGlance]. <br>		<table><tr><td colspan='2'>[[6e2h]] is a 3 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=6E2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2H FirstGlance]. <br>
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 6e2h" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6e2h" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Brunzelle, J S]]		[[Category: Brunzelle, J S]]
	[[Category: Couture, J F]]		[[Category: Couture, J F]]

OCA at 08:37, 17 October 2018

2018-10-17T08:37:45Z

←Older revision		Revision as of 08:37, 17 October 2018
Line 3:		Line 3:
	<StructureSection load='6e2h' size='340' side='right' caption='[[6e2h]], [[Resolution\|resolution]] 2.24Å' scene=''>		<StructureSection load='6e2h' size='340' side='right' caption='[[6e2h]], [[Resolution\|resolution]] 2.24Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6e2h]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2H FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6e2h]] is a 3 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=6E2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2H FirstGlance]. <br>
-	</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=6e2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2h OCA], [http://pdbe.org/6e2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e2h RCSB], [http://www.ebi.ac.uk/pdbsum/6e2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2h ProSAT]</span></td></tr>	+	</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]), DPY30 ([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=6e2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2h OCA], [http://pdbe.org/6e2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e2h RCSB], [http://www.ebi.ac.uk/pdbsum/6e2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2h 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/DPY30_HUMAN DPY30_HUMAN]] As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.<ref>PMID:19556245</ref> <ref>PMID:19651892</ref> <ref>PMID:21335234</ref>		[[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/DPY30_HUMAN DPY30_HUMAN]] As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.<ref>PMID:19556245</ref> <ref>PMID:19651892</ref> <ref>PMID:21335234</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Dpy-30 is a regulatory subunit controlling the histone methyltransferase activity of the KMT2 enzymes in vivo. Paradoxically, in vitro methyltransferase assays revealed that Dpy-30 only modestly participates in the positive heterotypic allosteric regulation of these methyltransferases. Detailed genome-wide, molecular and structural studies reveal that an extensive network of interactions taking place at the interface between Dpy-30 and Ash2L are critical for the correct placement, genome-wide, of H3K4me2 and H3K4me3 but marginally contribute to the methyltransferase activity of KMT2 enzymes in vitro. Moreover, we show that H3K4me2 peaks persisting following the loss of Dpy-30 are found in regions of highly transcribed genes, highlighting an interplay between Complex of Proteins Associated with SET1 (COMPASS) kinetics and the cycling of RNA polymerase to control H3K4 methylation. Overall, our data suggest that Dpy-30 couples its modest positive heterotypic allosteric regulation of KMT2 methyltransferase activity with its ability to help the positioning of SET1/COMPASS to control epigenetic signaling.
		+
		+	Structural Analysis of the Ash2L/Dpy-30 Complex Reveals a Heterogeneity in H3K4 Methylation.,Haddad JF, Yang Y, Takahashi YH, Joshi M, Chaudhary N, Woodfin AR, Benyoucef A, Yeung S, Brunzelle JS, Skiniotis G, Brand M, Shilatifard A, Couture JF Structure. 2018 Sep 27. pii: S0969-2126(18)30292-2. doi:, 10.1016/j.str.2018.08.004. PMID:30270175<ref>PMID:30270175</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6e2h" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Brunzelle, J S]]		[[Category: Brunzelle, J S]]
	[[Category: Couture, J F]]		[[Category: Couture, J F]]

OCA at 21:50, 9 August 2018

2018-08-09T21:50:06Z

←Older revision		Revision as of 21:50, 9 August 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6e2h ~~is ON HOLD~~	+	==Crystal structure of human Ash2L (SPRY domain and SDI motif) in complex with full length DPY-30==
-		+	<StructureSection load='6e2h' size='340' side='right' caption='[[6e2h]], [[Resolution\|resolution]] 2.24Å' scene=''>
-	~~Authors~~: ~~Joshi~~, M., ~~Brunzelle~~, J.S., ~~Couture~~, J.F.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6e2h]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2H FirstGlance]. <br>
-	~~Description~~: ~~Crystal structure~~ of ~~human Ash2L~~ (~~SPRY domain and SDI motif~~) in complex ~~with full length DPY~~-30	+	</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=6e2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2h OCA], [http://pdbe.org/6e2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e2h RCSB], [http://www.ebi.ac.uk/pdbsum/6e2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2h ProSAT]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
-	[[Category: Brunzelle, J.S]]	+	== Function ==
-	[[Category: Couture, J.F]]	+	[[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/DPY30_HUMAN DPY30_HUMAN]] As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.<ref>PMID:19556245</ref> <ref>PMID:19651892</ref> <ref>PMID:21335234</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Brunzelle, J S]]
		+	[[Category: Couture, J F]]
	[[Category: Joshi, M]]		[[Category: Joshi, M]]
		+	[[Category: Epigenetic]]
		+	[[Category: Histone]]
		+	[[Category: Lysine methylation]]
		+	[[Category: Mll]]
		+	[[Category: Nucleosome]]
		+	[[Category: Protein binding]]
		+	[[Category: Set1]]

OCA: Protected "6e2h" [edit=sysop:move=sysop]

2018-07-18T05:42:41Z

Protected "6e2h" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:42, 18 July 2018

OCA: New page: '''Unreleased structure''' The entry 6e2h is ON HOLD Authors: Joshi, M., Brunzelle, J.S., Couture, J.F. Description: Crystal structure of human Ash2L (SPRY domain and SDI motif) in com...

2018-07-18T05:42:39Z

New page: '''Unreleased structure''' The entry 6e2h is ON HOLD Authors: Joshi, M., Brunzelle, J.S., Couture, J.F. Description: Crystal structure of human Ash2L (SPRY domain and SDI motif) in com...

New page

'''Unreleased structure'''

The entry 6e2h is ON HOLD

Authors: Joshi, M., Brunzelle, J.S., Couture, J.F.

Description: Crystal structure of human Ash2L (SPRY domain and SDI motif) in complex with full length DPY-30
[[Category: Unreleased Structures]]
[[Category: Brunzelle, J.S]]
[[Category: Couture, J.F]]
[[Category: Joshi, M]]