6dv1 - Revision history

OCA at 14:36, 13 March 2024

OCA — Wed, 13 Mar 2024 14:36:59 GMT

←Older revision		Revision as of 14:36, 13 March 2024
Line 3:		Line 3:
	<StructureSection load='6dv1' size='340' side='right'caption='[[6dv1]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='6dv1' size='340' side='right'caption='[[6dv1]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6dv1]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DV1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6DV1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6dv1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DV1 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=BR:BROMIDE+ION'>BR</scene~~>, ~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~Ctnna1, Catna1 ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=10090 LK3 transgenic mice])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6dv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dv1 OCA], [~~http~~://pdbe.org/6dv1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6dv1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6dv1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6dv1 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=6dv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dv1 OCA], [https://pdbe.org/6dv1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dv1 RCSB], [https://www.ebi.ac.uk/pdbsum/6dv1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dv1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CTNA1_MOUSE CTNA1_MOUSE]] Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.<ref>PMID:16325583</ref>	+	[https://www.uniprot.org/uniprot/CTNA1_MOUSE CTNA1_MOUSE] Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.<ref>PMID:16325583</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	alpha-catenin is a key mechanosensor that forms force-dependent interactions with F-actin, thereby coupling the cadherin-catenin complex to the actin cytoskeleton at adherens junctions (AJs). However, the molecular mechanisms by which alpha-catenin engages F-actin under tension remained elusive. Here we show that the alpha1-helix of the alpha-catenin actin-binding domain (alphacat-ABD) is a mechanosensing motif that regulates tension-dependent F-actin binding and bundling. alphacat-ABD containing an alpha1-helix-unfolding mutation (H1) shows enhanced binding to F-actin in vitro. Although full-length alpha-catenin-H1 can generate epithelial monolayers that resist mechanical disruption, it fails to support normal AJ regulation in vivo. Structural and simulation analyses suggest that alpha1-helix allosterically controls the actin-binding residue V796 dynamics. Crystal structures of alphacat-ABD-H1 homodimer suggest that alpha-catenin can facilitate actin bundling while it remains bound to E-cadherin. We propose that force-dependent allosteric regulation of alphacat-ABD promotes dynamic interactions with F-actin involved in actin bundling, cadherin clustering, and AJ remodeling during tissue morphogenesis.	+
-		+
-	Force-dependent allostery of the alpha-catenin actin-binding domain controls adherens junction dynamics and functions.,Ishiyama N, Sarpal R, Wood MN, Barrick SK, Nishikawa T, Hayashi H, Kobb AB, Flozak AS, Yemelyanov A, Fernandez-Gonzalez R, Yonemura S, Leckband DE, Gottardi CJ, Tepass U, Ikura M Nat Commun. 2018 Nov 30;9(1):5121. doi: 10.1038/s41467-018-07481-7. PMID:30504777<ref>PMID:30504777</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 6dv1" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 27:		Line 18:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Ikura, M]]	+	[[Category: Ikura M]]
-	[[Category: Ishiyama, N]]	+	[[Category: Ishiyama N]]
-	~~[[Category: Cell adhesion]]~~	+
-	~~[[Category: F-actin-binding]]~~	+
-	~~[[Category: Five-helix bundle]]~~	+
-	~~[[Category: Mechanosensor~~]]	+

OCA at 08:55, 8 January 2020

OCA — Wed, 08 Jan 2020 08:55:01 GMT

←Older revision		Revision as of 08:55, 8 January 2020
Line 1:		Line 1:

	==Crystal structure of the alpha-E-catenin actin-binding domain==		==Crystal structure of the alpha-E-catenin actin-binding domain==
-	<StructureSection load='6dv1' size='340' side='right' caption='[[6dv1]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='6dv1' size='340' side='right'caption='[[6dv1]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6dv1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DV1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6dv1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DV1 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Ctnna1, Catna1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=6dv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dv1 OCA], [http://pdbe.org/6dv1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dv1 RCSB], [http://www.ebi.ac.uk/pdbsum/6dv1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dv1 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=6dv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dv1 OCA], [http://pdbe.org/6dv1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dv1 RCSB], [http://www.ebi.ac.uk/pdbsum/6dv1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dv1 ProSAT]</span></td></tr>
	</table>		</table>
Line 18:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 6dv1" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6dv1" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Catenin 3D structures\|Catenin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Lk3 transgenic mice]]
	[[Category: Ikura, M]]		[[Category: Ikura, M]]
	[[Category: Ishiyama, N]]		[[Category: Ishiyama, N]]

OCA at 08:24, 19 December 2018

OCA — Wed, 19 Dec 2018 08:24:42 GMT

←Older revision		Revision as of 08:24, 19 December 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6dv1 is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal structure of the alpha-E-catenin actin-binding domain==
		+	<StructureSection load='6dv1' size='340' side='right' caption='[[6dv1]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6dv1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DV1 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6dv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dv1 OCA], [http://pdbe.org/6dv1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dv1 RCSB], [http://www.ebi.ac.uk/pdbsum/6dv1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dv1 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CTNA1_MOUSE CTNA1_MOUSE]] Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.<ref>PMID:16325583</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	alpha-catenin is a key mechanosensor that forms force-dependent interactions with F-actin, thereby coupling the cadherin-catenin complex to the actin cytoskeleton at adherens junctions (AJs). However, the molecular mechanisms by which alpha-catenin engages F-actin under tension remained elusive. Here we show that the alpha1-helix of the alpha-catenin actin-binding domain (alphacat-ABD) is a mechanosensing motif that regulates tension-dependent F-actin binding and bundling. alphacat-ABD containing an alpha1-helix-unfolding mutation (H1) shows enhanced binding to F-actin in vitro. Although full-length alpha-catenin-H1 can generate epithelial monolayers that resist mechanical disruption, it fails to support normal AJ regulation in vivo. Structural and simulation analyses suggest that alpha1-helix allosterically controls the actin-binding residue V796 dynamics. Crystal structures of alphacat-ABD-H1 homodimer suggest that alpha-catenin can facilitate actin bundling while it remains bound to E-cadherin. We propose that force-dependent allosteric regulation of alphacat-ABD promotes dynamic interactions with F-actin involved in actin bundling, cadherin clustering, and AJ remodeling during tissue morphogenesis.

-	~~Authors: Ishiyama~~, N., ~~Ikura~~, M.	+	Force-dependent allostery of the alpha-catenin actin-binding domain controls adherens junction dynamics and functions.,Ishiyama N, Sarpal R, Wood MN, Barrick SK, Nishikawa T, Hayashi H, Kobb AB, Flozak AS, Yemelyanov A, Fernandez-Gonzalez R, Yonemura S, Leckband DE, Gottardi CJ, Tepass U, Ikura M Nat Commun. 2018 Nov 30;9(1):5121. doi: 10.1038/s41467-018-07481-7. PMID:30504777<ref>PMID:30504777</ref>

-	~~Description: Crystal structure~~ of the ~~alpha~~-E-~~catenin actin-binding domain~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
		+	<div class="pdbe-citations 6dv1" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Ikura, M]]		[[Category: Ikura, M]]
	[[Category: Ishiyama, N]]		[[Category: Ishiyama, N]]
		+	[[Category: Cell adhesion]]
		+	[[Category: F-actin-binding]]
		+	[[Category: Five-helix bundle]]
		+	[[Category: Mechanosensor]]

OCA at 05:49, 25 July 2018

OCA — Wed, 25 Jul 2018 05:49:47 GMT

←Older revision		Revision as of 05:49, 25 July 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6dv1 is ON HOLD	+	The entry 6dv1 is ON HOLD until Paper Publication

	Authors: Ishiyama, N., Ikura, M.		Authors: Ishiyama, N., Ikura, M.

OCA: Protected "6dv1" [edit=sysop:move=sysop]

OCA — Wed, 04 Jul 2018 05:43:31 GMT

Protected "6dv1" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:43, 4 July 2018

OCA: New page: '''Unreleased structure''' The entry 6dv1 is ON HOLD Authors: Ishiyama, N., Ikura, M. Description: Crystal structure of the alpha-E-catenin actin-binding domain [[Category: Unreleased ...

OCA — Wed, 04 Jul 2018 05:43:29 GMT

New page: '''Unreleased structure''' The entry 6dv1 is ON HOLD Authors: Ishiyama, N., Ikura, M. Description: Crystal structure of the alpha-E-catenin actin-binding domain [[Category: Unreleased ...

New page

'''Unreleased structure'''

The entry 6dv1 is ON HOLD

Authors: Ishiyama, N., Ikura, M.

Description: Crystal structure of the alpha-E-catenin actin-binding domain
[[Category: Unreleased Structures]]
[[Category: Ikura, M]]
[[Category: Ishiyama, N]]