3l6y: Difference between revisions
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==Crystal structure of p120 catenin in complex with E-cadherin== | ==Crystal structure of p120 catenin in complex with E-cadherin== | ||
<StructureSection load='3l6y' size='340' side='right' caption='[[3l6y]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='3l6y' size='340' side='right'caption='[[3l6y]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3l6y]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3l6y]] is a 6 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=3L6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L6Y FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=3l6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l6y OCA], [https://pdbe.org/3l6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l6y RCSB], [https://www.ebi.ac.uk/pdbsum/3l6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l6y ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CTND1_HUMAN CTND1_HUMAN] Binds to and inhibits the transcriptional repressor ZBTB33, which may lead to activation of target genes of the Wnt signaling pathway (By similarity). May associate with and regulate the cell adhesion properties of both C- and E-cadherins. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors. Promotes GLIS2 C-terminal cleavage.<ref>PMID:17344476</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l6/3l6y_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l6/3l6y_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3l6y" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3l6y" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Catenin 3D structures|Catenin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Ikura | [[Category: Large Structures]] | ||
[[Category: Ishiyama | [[Category: Ikura M]] | ||
[[Category: Lee | [[Category: Ishiyama N]] | ||
[[Category: Li | [[Category: Lee S-H]] | ||
[[Category: Liu | [[Category: Li G-Y]] | ||
[[Category: Reichardt | [[Category: Liu S]] | ||
[[Category: Smith | [[Category: Reichardt LF]] | ||
[[Category: Smith MJ]] | |||
Latest revision as of 11:32, 6 September 2023
Crystal structure of p120 catenin in complex with E-cadherinCrystal structure of p120 catenin in complex with E-cadherin
Structural highlights
FunctionCTND1_HUMAN Binds to and inhibits the transcriptional repressor ZBTB33, which may lead to activation of target genes of the Wnt signaling pathway (By similarity). May associate with and regulate the cell adhesion properties of both C- and E-cadherins. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors. Promotes GLIS2 C-terminal cleavage.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe association of p120 catenin (p120) with the juxtamembrane domain (JMD) of the cadherin cytoplasmic tail is critical for the surface stability of cadherin-catenin cell-cell adhesion complexes. Here, we present the crystal structure of p120 isoform 4A in complex with the JMD core region (JMD(core)) of E-cadherin. The p120 armadillo repeat domain contains modular binding pockets that are complementary to electrostatic and hydrophobic properties of the JMD(core). Single-residue mutations within the JMD(core)-binding site of p120 abolished its interaction with E- and N-cadherins in vitro and in cultured cells. These mutations of p120 enabled us to clearly differentiate between N-cadherin-dependent and -independent steps of neuronal dendritic spine morphogenesis crucial for synapse development. NMR studies revealed that p120 regulates the stability of cadherin-mediated cell-cell adhesion by associating with the majority of the JMD, including residues implicated in clathrin-mediated endocytosis and Hakai-dependent ubiquitination of E-cadherin, through its discrete "dynamic" and "static" binding sites. Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion.,Ishiyama N, Lee SH, Liu S, Li GY, Smith MJ, Reichardt LF, Ikura M Cell. 2010 Apr 2;141(1):117-28. PMID:20371349[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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