4b86 - Revision history

OCA at 10:57, 9 May 2024

OCA — Thu, 09 May 2024 10:57:53 GMT

←Older revision		Revision as of 10:57, 9 May 2024
Line 3:		Line 3:
	<StructureSection load='4b86' size='340' side='right'caption='[[4b86]], [[Resolution\|resolution]] 3.50Å' scene=''>		<StructureSection load='4b86' size='340' side='right'caption='[[4b86]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4b86]] is a 12 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=4B86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B86 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4b86]] is a 12 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=4B86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B86 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.5Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[4b7y\|4b7y]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b86 OCA], [https://pdbe.org/4b86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b86 RCSB], [https://www.ebi.ac.uk/pdbsum/4b86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b86 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=4b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b86 OCA], [https://pdbe.org/4b86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b86 RCSB], [https://www.ebi.ac.uk/pdbsum/4b86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b86 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/MSL1_HUMAN MSL1_HUMAN]] Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which is implicated in the formation of higher-order chromatin structure. Greatly enhances MSL2 E3 ubiquitin ligase activity, promoting monoubiquitination of histone H2B at 'Lys-34' (H2BK34Ub). This modification in turn stimulates histone H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. In the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together for enzymatic activity regulation.<ref>PMID:16227571</ref> <ref>PMID:21726816</ref> <ref>PMID:22547026</ref> [[https://www.uniprot.org/uniprot/MSL2_HUMAN MSL2_HUMAN]] Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure. Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histine H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1.<ref>PMID:21726816</ref>	+	[https://www.uniprot.org/uniprot/MSL1_HUMAN MSL1_HUMAN] Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which is implicated in the formation of higher-order chromatin structure. Greatly enhances MSL2 E3 ubiquitin ligase activity, promoting monoubiquitination of histone H2B at 'Lys-34' (H2BK34Ub). This modification in turn stimulates histone H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. In the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together for enzymatic activity regulation.<ref>PMID:16227571</ref> <ref>PMID:21726816</ref> <ref>PMID:22547026</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Akhtar, A]]	+	[[Category: Akhtar A]]
-	[[Category: Cusack, S]]	+	[[Category: Cusack S]]
-	[[Category: Georgiev, P]]	+	[[Category: Georgiev P]]
-	[[Category: Hallacli, E]]	+	[[Category: Hallacli E]]
-	[[Category: Kadlec, J]]	+	[[Category: Kadlec J]]
-	[[Category: Lipp, M]]	+	[[Category: Lipp M]]
-	[[Category: Spielman, C]]	+	[[Category: Spielman C]]
-	~~[[Category: Chromatin]]~~	+
-	~~[[Category: Dosage compensation]]~~	+
-	~~[[Category: Gene regulation~~]]	+

OCA at 07:03, 31 August 2022

OCA — Wed, 31 Aug 2022 07:03:17 GMT

←Older revision		Revision as of 07:03, 31 August 2022
Line 3:		Line 3:
	<StructureSection load='4b86' size='340' side='right'caption='[[4b86]], [[Resolution\|resolution]] 3.50Å' scene=''>		<StructureSection load='4b86' size='340' side='right'caption='[[4b86]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4b86]] is a 12 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=4B86 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4B86 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4b86]] is a 12 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=4B86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B86 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4b7y\|4b7y]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b7y\|4b7y]]</div></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=4b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b86 OCA], [~~http~~://pdbe.org/4b86 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4b86 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4b86 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4b86 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=4b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b86 OCA], [https://pdbe.org/4b86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b86 RCSB], [https://www.ebi.ac.uk/pdbsum/4b86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b86 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/MSL1_HUMAN MSL1_HUMAN]] Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which is implicated in the formation of higher-order chromatin structure. Greatly enhances MSL2 E3 ubiquitin ligase activity, promoting monoubiquitination of histone H2B at 'Lys-34' (H2BK34Ub). This modification in turn stimulates histone H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. In the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together for enzymatic activity regulation.<ref>PMID:16227571</ref> <ref>PMID:21726816</ref> <ref>PMID:22547026</ref> [[~~http~~://www.uniprot.org/uniprot/MSL2_HUMAN MSL2_HUMAN]] Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure. Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histine H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1.<ref>PMID:21726816</ref>	+	[[https://www.uniprot.org/uniprot/MSL1_HUMAN MSL1_HUMAN]] Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which is implicated in the formation of higher-order chromatin structure. Greatly enhances MSL2 E3 ubiquitin ligase activity, promoting monoubiquitination of histone H2B at 'Lys-34' (H2BK34Ub). This modification in turn stimulates histone H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. In the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together for enzymatic activity regulation.<ref>PMID:16227571</ref> <ref>PMID:21726816</ref> <ref>PMID:22547026</ref> [[https://www.uniprot.org/uniprot/MSL2_HUMAN MSL2_HUMAN]] Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure. Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histine H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1.<ref>PMID:21726816</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 13:54, 13 March 2019

OCA — Wed, 13 Mar 2019 13:54:17 GMT

←Older revision		Revision as of 13:54, 13 March 2019
Line 1:		Line 1:

	==Crystal structure of the MSL1-MSL2 complex (3.5A)==		==Crystal structure of the MSL1-MSL2 complex (3.5A)==
-	<StructureSection load='4b86' size='340' side='right' caption='[[4b86]], [[Resolution\|resolution]] 3.50Å' scene=''>	+	<StructureSection load='4b86' size='340' side='right'caption='[[4b86]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4b86]] is a 12 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=4B86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B86 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4b86]] is a 12 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=4B86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B86 FirstGlance]. <br>
Line 24:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Akhtar, A]]		[[Category: Akhtar, A]]
	[[Category: Cusack, S]]		[[Category: Cusack, S]]

OCA at 03:41, 5 August 2016

OCA — Fri, 05 Aug 2016 03:41:46 GMT

←Older revision		Revision as of 03:41, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the MSL1-MSL2 complex (3.5A)==		==Crystal structure of the MSL1-MSL2 complex (3.5A)==
	<StructureSection load='4b86' size='340' side='right' caption='[[4b86]], [[Resolution\|resolution]] 3.50Å' scene=''>		<StructureSection load='4b86' size='340' side='right' caption='[[4b86]], [[Resolution\|resolution]] 3.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4b86]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Buakea_kaeuae Buakea kaeuae] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B86 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4b86]] is a 12 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=4B86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B86 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4b7y\|4b7y]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4b7y\|4b7y]]</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=4b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b86 RCSB], [http://www.ebi.ac.uk/pdbsum/4b86 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=4b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b86 OCA], [http://pdbe.org/4b86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b86 RCSB], [http://www.ebi.ac.uk/pdbsum/4b86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b86 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 4b86" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Buakea kaeuae]]~~	+	[[Category: Human]]
-	~~[[Category: Homo sapiens~~]]	+
	[[Category: Akhtar, A]]		[[Category: Akhtar, A]]
	[[Category: Cusack, S]]		[[Category: Cusack, S]]

OCA at 15:34, 25 December 2014

OCA — Thu, 25 Dec 2014 15:34:02 GMT

←Older revision		Revision as of 15:34, 25 December 2014
Line 7:		Line 7:
	<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=4b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b86 RCSB], [http://www.ebi.ac.uk/pdbsum/4b86 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=4b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b86 RCSB], [http://www.ebi.ac.uk/pdbsum/4b86 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MSL1_HUMAN MSL1_HUMAN]] Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which is implicated in the formation of higher-order chromatin structure. Greatly enhances MSL2 E3 ubiquitin ligase activity, promoting monoubiquitination of histone H2B at 'Lys-34' (H2BK34Ub). This modification in turn stimulates histone H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. In the MSL complex, acts as a scaffold to tether MSL3 and KAT8 together for enzymatic activity regulation.<ref>PMID:16227571</ref> <ref>PMID:21726816</ref> <ref>PMID:22547026</ref> [[http://www.uniprot.org/uniprot/MSL2_HUMAN MSL2_HUMAN]] Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure. Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histine H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1.<ref>PMID:21726816</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 16:07, 9 December 2014

OCA — Tue, 09 Dec 2014 16:07:19 GMT

←Older revision		Revision as of 16:07, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4b86.~~jpg~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of the MSL1-MSL2 complex (3.5A)==
		+	<StructureSection load='4b86' size='340' side='right' caption='[[4b86]], [[Resolution\|resolution]] 3.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4b86]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Buakea_kaeuae Buakea kaeuae] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B86 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4b7y\|4b7y]]</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=4b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b86 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b86 RCSB], [http://www.ebi.ac.uk/pdbsum/4b86 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The Male-Specific Lethal (MSL) complex regulates dosage compensation of the male X chromosome in Drosophila. Here, we report the crystal structure of its MSL1/MSL2 core, where two MSL2 subunits bind to a dimer formed by two molecules of MSL1. Analysis of structure-based mutants revealed that MSL2 can only interact with the MSL1 dimer, but MSL1 dimerization is MSL2 independent. We show that Msl1 is a substrate for Msl2 E3 ubiquitin ligase activity. ChIP experiments revealed that Msl1 dimerization is essential for targeting and spreading of the MSL complex on X-linked genes; however, Msl1 binding to promoters of male and female cells is independent of the dimer status and other MSL proteins. Finally, we show that loss of Msl1 dimerization leads to male-specific lethality. We propose that Msl1-mediated dimerization of the entire MSL complex is required for Msl2 binding, X chromosome recognition, and spreading along the X chromosome.

-	~~{{STRUCTURE_4b86\| PDB=4b86 \| SCENE= }}~~	+	Msl1-mediated dimerization of the dosage compensation complex is essential for male X-chromosome regulation in Drosophila.,Hallacli E, Lipp M, Georgiev P, Spielman C, Cusack S, Akhtar A, Kadlec J Mol Cell. 2012 Nov 30;48(4):587-600. doi: 10.1016/j.molcel.2012.09.014. Epub 2012, Oct 18. PMID:23084835<ref>PMID:23084835</ref>

-	~~===Crystal structure~~ of the ~~MSL1-MSL2 complex (3~~.~~5A)===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_23084835}}~~	+	== References ==
-		+	<references/>
-	==~~About this Structure~~==	+	__TOC__
-	~~[[4b86]] is a 12 chain structure with sequence from [http:~~//en.wikipedia.org/wiki/Buakea_kaeuae Buakea kaeuae] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B86 OCA].	+	</StructureSection>
	[[Category: Buakea kaeuae]]		[[Category: Buakea kaeuae]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Akhtar, A.]]	+	[[Category: Akhtar, A]]
-	[[Category: Cusack, S.]]	+	[[Category: Cusack, S]]
-	[[Category: Georgiev, P.]]	+	[[Category: Georgiev, P]]
-	[[Category: Hallacli, E.]]	+	[[Category: Hallacli, E]]
-	[[Category: Kadlec, J.]]	+	[[Category: Kadlec, J]]
-	[[Category: Lipp, M.]]	+	[[Category: Lipp, M]]
-	[[Category: Spielman, C.]]	+	[[Category: Spielman, C]]
	[[Category: Chromatin]]		[[Category: Chromatin]]
	[[Category: Dosage compensation]]		[[Category: Dosage compensation]]
	[[Category: Gene regulation]]		[[Category: Gene regulation]]

OCA at 12:55, 6 February 2013

OCA — Wed, 06 Feb 2013 12:55:58 GMT

←Older revision		Revision as of 12:55, 6 February 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4b86.jpg\|left\|200px]]

-	~~The entry~~ 4b86 ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4b86\| PDB=4b86 \| SCENE= }}

-	~~Authors: Hallacli, E., Lipp, M., Georgiev, P., Spielman, C., Cusack, S., Akhtar, A., Kadlec, J~~.	+	===Crystal structure of the MSL1-MSL2 complex (3.5A)===

-	~~Description: Crystal~~ structure ~~of the MSL1~~-~~MSL2 complex (3~~.~~5A)~~	+	{{ABSTRACT_PUBMED_23084835}}
		+
		+	==About this Structure==
		+	[[4b86]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Buakea_kaeuae Buakea kaeuae] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B86 OCA].
		+	[[Category: Buakea kaeuae]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Akhtar, A.]]
		+	[[Category: Cusack, S.]]
		+	[[Category: Georgiev, P.]]
		+	[[Category: Hallacli, E.]]
		+	[[Category: Kadlec, J.]]
		+	[[Category: Lipp, M.]]
		+	[[Category: Spielman, C.]]
		+	[[Category: Chromatin]]
		+	[[Category: Dosage compensation]]
		+	[[Category: Gene regulation]]

OCA at 06:43, 19 September 2012

OCA — Wed, 19 Sep 2012 06:43:49 GMT

←Older revision		Revision as of 06:43, 19 September 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4b86 is ON HOLD	+	The entry 4b86 is ON HOLD until Paper Publication

	Authors: Hallacli, E., Lipp, M., Georgiev, P., Spielman, C., Cusack, S., Akhtar, A., Kadlec, J.		Authors: Hallacli, E., Lipp, M., Georgiev, P., Spielman, C., Cusack, S., Akhtar, A., Kadlec, J.

-	Description: Crystal structure of the MSL1-MSL2 complex	+	Description: Crystal structure of the MSL1-MSL2 complex (3.5A)

OCA at 04:44, 5 September 2012

OCA — Wed, 05 Sep 2012 04:44:15 GMT

←Older revision		Revision as of 04:44, 5 September 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4b86 is ON HOLD ~~until sometime in the future~~	+	The entry 4b86 is ON HOLD

	Authors: Hallacli, E., Lipp, M., Georgiev, P., Spielman, C., Cusack, S., Akhtar, A., Kadlec, J.		Authors: Hallacli, E., Lipp, M., Georgiev, P., Spielman, C., Cusack, S., Akhtar, A., Kadlec, J.

	Description: Crystal structure of the MSL1-MSL2 complex		Description: Crystal structure of the MSL1-MSL2 complex

OCA: Protected "4b86" [edit=sysop:move=sysop]

OCA — Wed, 29 Aug 2012 04:36:55 GMT

Protected "4b86" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:36, 29 August 2012