5suz - Revision history

OCA at 15:33, 6 March 2024

OCA — Wed, 06 Mar 2024 15:33:28 GMT

←Older revision		Revision as of 15:33, 6 March 2024
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	<StructureSection load='5suz' size='340' side='right'caption='[[5suz]], [[Resolution\|resolution]] 1.84Å' scene=''>		<StructureSection load='5suz' size='340' side='right'caption='[[5suz]], [[Resolution\|resolution]] 1.84Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5suz]] 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=5SUZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5SUZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5suz]] 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=5SUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SUZ FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 1.84Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~DVL2 ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5suz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5suz OCA], [~~http~~://pdbe.org/5suz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5suz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5suz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5suz 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=5suz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5suz OCA], [https://pdbe.org/5suz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5suz RCSB], [https://www.ebi.ac.uk/pdbsum/5suz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5suz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DVL2_HUMAN DVL2_HUMAN]] Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes (By similarity).<ref>PMID:19252499</ref>	+	[https://www.uniprot.org/uniprot/DVL2_HUMAN DVL2_HUMAN] Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes (By similarity).<ref>PMID:19252499</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Extracellular signals are often transduced by dynamic signaling complexes ("signalosomes") assembled by oligomerizing hub proteins following their recruitment to signal-activated transmembrane receptors. A paradigm is the Wnt signalosome, which is assembled by Dishevelled via reversible head-to-tail polymerization by its DIX domain. Its activity causes stabilization of beta-catenin, a Wnt effector with pivotal roles in animal development and cancer. How Wnt triggers signalosome assembly is unknown. Here, we use structural analysis, as well as biophysical and cell-based assays, to show that the DEP domain of Dishevelled undergoes a conformational switch, from monomeric to swapped dimer, to trigger DIX-dependent polymerization and signaling to beta-catenin. This occurs in two steps: binding of monomeric DEP to Frizzled followed by DEP domain swapping triggered by its high local concentration upon Wnt-induced recruitment into clathrin-coated pits. DEP domain swapping confers directional bias on signaling, and the dimerization provides cross-linking between Dishevelled polymers, illustrating a key principle underlying signalosome formation.	+
-		+
-	Wnt Signalosome Assembly by DEP Domain Swapping of Dishevelled.,Gammons MV, Renko M, Johnson CM, Rutherford TJ, Bienz M Mol Cell. 2016 Oct 6;64(1):92-104. doi: 10.1016/j.molcel.2016.08.026. Epub 2016, Sep 29. PMID:27692984<ref>PMID:27692984</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 5suz" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bienz, M]]	+	[[Category: Bienz M]]
-	[[Category: Gammons~~, M V~~]]	+	[[Category: Gammons MV]]
-	[[Category: Renko, M]]	+	[[Category: Renko M]]
-	~~[[Category: Dep domain]]~~	+
-	~~[[Category: Dishevelled]]~~	+
-	~~[[Category: Signaling protein]]~~	+
-	~~[[Category: Wnt signalling~~]]	+

OCA at 11:11, 16 September 2020

OCA — Wed, 16 Sep 2020 11:11:52 GMT

←Older revision		Revision as of 11:11, 16 September 2020
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	==Domain-swapped dimer of human Dishevelled2 DEP domain: C-centered monoclinic crystal form crystallised from monomeric fraction==		==Domain-swapped dimer of human Dishevelled2 DEP domain: C-centered monoclinic crystal form crystallised from monomeric fraction==
-	<StructureSection load='5suz' size='340' side='right' caption='[[5suz]], [[Resolution\|resolution]] 1.84Å' scene=''>	+	<StructureSection load='5suz' size='340' side='right'caption='[[5suz]], [[Resolution\|resolution]] 1.84Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5suz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SUZ OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5SUZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5suz]] 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=5SUZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5SUZ FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5suz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5suz OCA], [http://pdbe.org/5suz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5suz RCSB], [http://www.ebi.ac.uk/pdbsum/5suz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5suz ProSAT]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DVL2 ([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://proteopedia.org/fgij/fg.htm?mol=5suz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5suz OCA], [http://pdbe.org/5suz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5suz RCSB], [http://www.ebi.ac.uk/pdbsum/5suz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5suz ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bienz, M]]		[[Category: Bienz, M]]
	[[Category: Gammons, M V]]		[[Category: Gammons, M V]]

OCA at 09:52, 19 October 2016

OCA — Wed, 19 Oct 2016 09:52:43 GMT

←Older revision		Revision as of 09:52, 19 October 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5suz is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Domain-swapped dimer of human Dishevelled2 DEP domain: C-centered monoclinic crystal form crystallised from monomeric fraction==
		+	<StructureSection load='5suz' size='340' side='right' caption='[[5suz]], [[Resolution\|resolution]] 1.84Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5suz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SUZ FirstGlance]. <br>
		+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5suz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5suz OCA], [http://pdbe.org/5suz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5suz RCSB], [http://www.ebi.ac.uk/pdbsum/5suz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5suz ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DVL2_HUMAN DVL2_HUMAN]] Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes (By similarity).<ref>PMID:19252499</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Extracellular signals are often transduced by dynamic signaling complexes ("signalosomes") assembled by oligomerizing hub proteins following their recruitment to signal-activated transmembrane receptors. A paradigm is the Wnt signalosome, which is assembled by Dishevelled via reversible head-to-tail polymerization by its DIX domain. Its activity causes stabilization of beta-catenin, a Wnt effector with pivotal roles in animal development and cancer. How Wnt triggers signalosome assembly is unknown. Here, we use structural analysis, as well as biophysical and cell-based assays, to show that the DEP domain of Dishevelled undergoes a conformational switch, from monomeric to swapped dimer, to trigger DIX-dependent polymerization and signaling to beta-catenin. This occurs in two steps: binding of monomeric DEP to Frizzled followed by DEP domain swapping triggered by its high local concentration upon Wnt-induced recruitment into clathrin-coated pits. DEP domain swapping confers directional bias on signaling, and the dimerization provides cross-linking between Dishevelled polymers, illustrating a key principle underlying signalosome formation.

-	~~Authors: Renko, M~~., Gammons, M~~.V.~~, ~~Bienz~~, M.	+	Wnt Signalosome Assembly by DEP Domain Swapping of Dishevelled.,Gammons MV, Renko M, Johnson CM, Rutherford TJ, Bienz M Mol Cell. 2016 Oct 6;64(1):92-104. doi: 10.1016/j.molcel.2016.08.026. Epub 2016, Sep 29. PMID:27692984<ref>PMID:27692984</ref>

-	~~Description: Domain-swapped dimer~~ of ~~human Dishevelled2 DEP domain: C-centered monoclinic crystal form crystallised from monomeric fraction~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
		+	<div class="pdbe-citations 5suz" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Bienz, M]]		[[Category: Bienz, M]]
-	[[Category: Gammons, M.V]]	+	[[Category: Gammons, M V]]
	[[Category: Renko, M]]		[[Category: Renko, M]]
		+	[[Category: Dep domain]]
		+	[[Category: Dishevelled]]
		+	[[Category: Signaling protein]]
		+	[[Category: Wnt signalling]]

OCA at 15:18, 9 September 2016

OCA — Fri, 09 Sep 2016 15:18:21 GMT

←Older revision		Revision as of 15:18, 9 September 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Renko, M., Gammons, M.V., Bienz, M.		Authors: Renko, M., Gammons, M.V., Bienz, M.

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

OCA — Wed, 10 Aug 2016 14:43:33 GMT

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

←Older revision

Revision as of 14:43, 10 August 2016

OCA: New page: '''Unreleased structure''' The entry 5suz is ON HOLD Authors: Renko, M., Gammons, M.V., Bienz, M. Description: Domain-swapped dimer of human Dishevelled2 DEP domain: C-centered monocli...

OCA — Wed, 10 Aug 2016 14:43:32 GMT

New page: '''Unreleased structure''' The entry 5suz is ON HOLD Authors: Renko, M., Gammons, M.V., Bienz, M. Description: Domain-swapped dimer of human Dishevelled2 DEP domain: C-centered monocli...

New page

'''Unreleased structure'''

The entry 5suz is ON HOLD

Authors: Renko, M., Gammons, M.V., Bienz, M.

Description: Domain-swapped dimer of human Dishevelled2 DEP domain: C-centered monoclinic crystal form crystallised from monomeric fraction
[[Category: Unreleased Structures]]
[[Category: Bienz, M]]
[[Category: Gammons, M.V]]
[[Category: Renko, M]]