4r11 - Revision history

OCA at 14:04, 22 February 2023

OCA — Wed, 22 Feb 2023 14:04:24 GMT

←Older revision		Revision as of 14:04, 22 February 2023
Line 3:		Line 3:
	<StructureSection load='4r11' size='340' side='right'caption='[[4r11]], [[Resolution\|resolution]] 2.79Å' scene=''>		<StructureSection load='4r11' size='340' side='right'caption='[[4r11]], [[Resolution\|resolution]] 2.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r11]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Caeel Caeel~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R11 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4R11 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r11]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R11 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=4r11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r11 OCA], [https://pdbe.org/4r11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r11 RCSB], [https://www.ebi.ac.uk/pdbsum/4r11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r11 ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4r0z\|4r0z]], [[4r10\|4r10]]</td></tr>~~	+
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hmp-2, K05C4.6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL]), hmr-1, W02B9.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=4r11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r11 OCA], [~~http~~://pdbe.org/4r11 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4r11 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4r11 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4r11 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/HMP2_CAEEL HMP2_CAEEL]] Required for cell migration during body enclosure and cell shape changes during body elongation.<ref>PMID:9531567</ref> [[http://www.uniprot.org/uniprot/HMR1_CAEEL HMR1_CAEEL]] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Isoform A is required for cell migration during body enclosure and cell shape changes during body elongation. Required for proper localization of other junctional components, such as hmp-1, hmp-2 and jac-1. Isoform b is involved in axonal guidance in a subset of motor neurons.<ref>PMID:11790304</ref> <ref>PMID:12847081</ref> <ref>PMID:9531567</ref>	+	[https://www.uniprot.org/uniprot/HMP2_CAEEL HMP2_CAEEL] Required for cell migration during body enclosure and cell shape changes during body elongation.<ref>PMID:9531567</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Caeel~~]]	+	[[Category: Caenorhabditis elegans]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bang, I]]	+	[[Category: Bang I]]
-	[[Category: Choi, H J]]	+	[[Category: Choi H-J]]
-	[[Category: Hardin, J]]	+	[[Category: Hardin J]]
-	[[Category: Loveless, T]]	+	[[Category: Loveless T]]
-	[[Category: Lynch, A]]	+	[[Category: Lynch A]]
-	[[Category: Weis~~, W I]]~~	+	[[Category: Weis WI]]
-	~~[[Category: Armadillo repeat]]~~	+
-	~~[[Category: Cell adhesion]]~~	+
-	~~[[Category: Cell adhesion-protein binding complex]]~~	+
-	~~[[Category: Phosphorylation~~]]	+

OCA at 09:11, 24 April 2019

OCA — Wed, 24 Apr 2019 09:11:46 GMT

←Older revision		Revision as of 09:11, 24 April 2019
Line 1:		Line 1:

	==A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo==		==A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo==
-	<StructureSection load='4r11' size='340' side='right' caption='[[4r11]], [[Resolution\|resolution]] 2.79Å' scene=''>	+	<StructureSection load='4r11' size='340' side='right'caption='[[4r11]], [[Resolution\|resolution]] 2.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r11]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R11 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R11 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r11]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R11 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R11 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4r0z\|4r0z]], [[4r10\|4r10]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4r0z\|4r0z]], [[4r10\|4r10]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hmp-2, K05C4.6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL]), hmr-1, W02B9.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=4r11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r11 OCA], [http://pdbe.org/4r11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r11 RCSB], [http://www.ebi.ac.uk/pdbsum/4r11 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r11 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=4r11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r11 OCA], [http://pdbe.org/4r11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r11 RCSB], [http://www.ebi.ac.uk/pdbsum/4r11 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r11 ProSAT]</span></td></tr>
	</table>		</table>
Line 24:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Caeel]]
		+	[[Category: Large Structures]]
	[[Category: Bang, I]]		[[Category: Bang, I]]
	[[Category: Choi, H J]]		[[Category: Choi, H J]]

OCA at 18:34, 1 February 2017

OCA — Wed, 01 Feb 2017 18:34:42 GMT

←Older revision		Revision as of 18:34, 1 February 2017
Line 1:		Line 1:
		+
	==A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo==		==A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo==
	<StructureSection load='4r11' size='340' side='right' caption='[[4r11]], [[Resolution\|resolution]] 2.79Å' scene=''>		<StructureSection load='4r11' size='340' side='right' caption='[[4r11]], [[Resolution\|resolution]] 2.79Å' scene=''>
Line 6:		Line 7:
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4r0z\|4r0z]], [[4r10\|4r10]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4r0z\|4r0z]], [[4r10\|4r10]]</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=4r11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r11 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r11 RCSB], [http://www.ebi.ac.uk/pdbsum/4r11 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=4r11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r11 OCA], [http://pdbe.org/4r11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r11 RCSB], [http://www.ebi.ac.uk/pdbsum/4r11 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r11 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4r11" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:34, 30 April 2015

OCA — Thu, 30 Apr 2015 11:34:11 GMT

←Older revision		Revision as of 11:34, 30 April 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo==
		+	<StructureSection load='4r11' size='340' side='right' caption='[[4r11]], [[Resolution\|resolution]] 2.79Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4r11]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R11 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R11 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4r0z\|4r0z]], [[4r10\|4r10]]</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=4r11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r11 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r11 RCSB], [http://www.ebi.ac.uk/pdbsum/4r11 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HMP2_CAEEL HMP2_CAEEL]] Required for cell migration during body enclosure and cell shape changes during body elongation.<ref>PMID:9531567</ref> [[http://www.uniprot.org/uniprot/HMR1_CAEEL HMR1_CAEEL]] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Isoform A is required for cell migration during body enclosure and cell shape changes during body elongation. Required for proper localization of other junctional components, such as hmp-1, hmp-2 and jac-1. Isoform b is involved in axonal guidance in a subset of motor neurons.<ref>PMID:11790304</ref> <ref>PMID:12847081</ref> <ref>PMID:9531567</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	In metazoan adherens junctions, beta-catenin links the cytoplasmic tail of classical cadherins to the F-actin-binding protein alpha-catenin. Phosphorylation of a Ser/Thr-rich region in the cadherin tail dramatically enhances affinity for beta-catenin and promotes cell-cell adhesion in cell culture systems, but its importance has not been demonstrated in vivo. Here, we identify a critical phosphorylated serine in the C. elegans cadherin HMR-1 required for strong binding to the beta-catenin homolog HMP-2. Ablation of this phosphoserine interaction produces developmental defects that resemble full loss-of-function (Hammerhead and Humpback) phenotypes. Most metazoans possess a single gene for beta-catenin, which is also a transcriptional coactivator in Wnt signaling. Nematodes and planaria, however, have a set of paralogous beta-catenins; for example, C. elegans HMP-2 functions only in cell-cell adhesion, whereas SYS-1 mediates transcriptional activation through interactions with POP-1/Tcf. Our structural data define critical sequence differences responsible for the unique ligand specificities of these two proteins.

-	~~The entry 4r11 is ON HOLD until Paper Publication~~	+	A Conserved Phosphorylation Switch Controls the Interaction between Cadherin and beta-Catenin In Vitro and In Vivo.,Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI Dev Cell. 2015 Apr 6;33(1):82-93. doi: 10.1016/j.devcel.2015.02.005. PMID:25850673<ref>PMID:25850673</ref>

-	~~Authors: Choi~~, H.-J.~~, Loveless, T., Lynch, A., Bang, I., Hardin, J., Weis, W.I~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
-	[[Category: ~~Lynch~~, A]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Bang, I]]
		+	[[Category: Choi, H J]]
	[[Category: Hardin, J]]		[[Category: Hardin, J]]
	[[Category: Loveless, T]]		[[Category: Loveless, T]]
-	[[Category: ~~Bang~~, I]]	+	[[Category: Lynch, A]]
-	[[Category: ~~Choi~~, H.-J]]	+	[[Category: Weis, W I]]
-	[[Category: ~~Weis, W.I~~]]	+	[[Category: Armadillo repeat]]
		+	[[Category: Cell adhesion]]
		+	[[Category: Cell adhesion-protein binding complex]]
		+	[[Category: Phosphorylation]]

OCA at 16:22, 24 December 2014

OCA — Wed, 24 Dec 2014 16:22:16 GMT

←Older revision		Revision as of 16:22, 24 December 2014
Line 6:		Line 6:

	Description: A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo		Description: A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo
		+	[[Category: Unreleased Structures]]
		+	[[Category: Lynch, A]]
		+	[[Category: Hardin, J]]
		+	[[Category: Loveless, T]]
		+	[[Category: Bang, I]]
		+	[[Category: Choi, H.-J]]
		+	[[Category: Weis, W.I]]

OCA at 08:20, 10 September 2014

OCA — Wed, 10 Sep 2014 08:20:40 GMT

←Older revision		Revision as of 08:20, 10 September 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4r11 is ON HOLD	+	The entry 4r11 is ON HOLD until Paper Publication

	Authors: Choi, H.-J., Loveless, T., Lynch, A., Bang, I., Hardin, J., Weis, W.I.		Authors: Choi, H.-J., Loveless, T., Lynch, A., Bang, I., Hardin, J., Weis, W.I.

	Description: A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo		Description: A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo

OCA at 06:55, 27 August 2014

OCA — Wed, 27 Aug 2014 06:55:56 GMT

←Older revision		Revision as of 06:55, 27 August 2014
Line 5:		Line 5:
	Authors: Choi, H.-J., Loveless, T., Lynch, A., Bang, I., Hardin, J., Weis, W.I.		Authors: Choi, H.-J., Loveless, T., Lynch, A., Bang, I., Hardin, J., Weis, W.I.

-	Description: A conserved phosphorylation switch controls the interaction between cadherin and -catenin in vitro and in vivo	+	Description: A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo

OCA: Protected "4r11" [edit=sysop:move=sysop]

OCA — Wed, 13 Aug 2014 07:47:43 GMT

Protected "4r11" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:47, 13 August 2014

OCA: New page: '''Unreleased structure''' The entry 4r11 is ON HOLD Authors: Choi, H.-J., Loveless, T., Lynch, A., Bang, I., Hardin, J., Weis, W.I. Description: A conserved phosphorylation switch con...

OCA — Wed, 13 Aug 2014 07:47:41 GMT

New page: '''Unreleased structure''' The entry 4r11 is ON HOLD Authors: Choi, H.-J., Loveless, T., Lynch, A., Bang, I., Hardin, J., Weis, W.I. Description: A conserved phosphorylation switch con...

New page

'''Unreleased structure'''

The entry 4r11 is ON HOLD

Authors: Choi, H.-J., Loveless, T., Lynch, A., Bang, I., Hardin, J., Weis, W.I.

Description: A conserved phosphorylation switch controls the interaction between cadherin and -catenin in vitro and in vivo