3l6x

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of p120 catenin in complex with E-cadherin

Structural highlights

3l6x is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[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 PubMed

The 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.

References

↑ Hosking CR, Ulloa F, Hogan C, Ferber EC, Figueroa A, Gevaert K, Birchmeier W, Briscoe J, Fujita Y. The transcriptional repressor Glis2 is a novel binding partner for p120 catenin. Mol Biol Cell. 2007 May;18(5):1918-27. Epub 2007 Mar 7. PMID:17344476 doi:10.1091/mbc.E06-10-0941
↑ Ishiyama N, Lee SH, Liu S, Li GY, Smith MJ, Reichardt LF, Ikura M. Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion. Cell. 2010 Apr 2;141(1):117-28. PMID:20371349 doi:10.1016/j.cell.2010.01.017

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3l6x"

@@ Line 1: / Line 1: @@
 ==Crystal structure of p120 catenin in complex with E-cadherin==
-<StructureSection load='3l6x' size='340' side='right' caption='[[3l6x]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='3l6x' size='340' side='right'caption='[[3l6x]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3l6x]] 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=3L6X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L6X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3l6x]] 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=3L6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L6X FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.4&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l6y|3l6y]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTNND1, KIAA0384 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3l6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l6x OCA], [https://pdbe.org/3l6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l6x RCSB], [https://www.ebi.ac.uk/pdbsum/3l6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l6x 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=3l6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l6x OCA], [http://pdbe.org/3l6x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l6x RCSB], [http://www.ebi.ac.uk/pdbsum/3l6x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l6x ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l6/3l6x_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l6/3l6x_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 29: @@
 </div>
 <div class="pdbe-citations 3l6x" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Catenin 3D structures|Catenin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Ikura, M]]
+[[Category: Large Structures]]
-[[Category: Ishiyama, N]]
+[[Category: Ikura M]]
-[[Category: Lee, S H]]
+[[Category: Ishiyama N]]
-[[Category: Li, G Y]]
+[[Category: Lee S-H]]
-[[Category: Liu, S]]
+[[Category: Li G-Y]]
-[[Category: Reichardt, L F]]
+[[Category: Liu S]]
-[[Category: Smith, M J]]
+[[Category: Reichardt LF]]
-[[Category: Arm]]
+[[Category: Smith MJ]]
-[[Category: Armadillo]]
-[[Category: Arvcf]]
-[[Category: Cadherin]]
-[[Category: Catenin]]
-[[Category: Cell adhesion]]
-[[Category: Cell membrane]]
-[[Category: Cell-cell adhesion]]
-[[Category: Complex]]
-[[Category: Delta-catenin]]
-[[Category: Dp120]]
-[[Category: E-cadherin]]
-[[Category: Jac-1]]
-[[Category: Jmd]]
-[[Category: Membrane]]
-[[Category: Nucleus]]
-[[Category: P0071]]
-[[Category: P120]]
-[[Category: Phosphoprotein]]
-[[Category: Transcription]]
-[[Category: Transcription regulation]]
-[[Category: Wnt signaling pathway]]

3l6x

From Proteopedia

Current revision

Crystal structure of p120 catenin in complex with E-cadherin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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