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PDBsum entry 3l6y
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protein Protein-protein interface(s) links
Cell adhesion PDB id
3l6y

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
356 a.a. *
18 a.a. *
376 a.a. *
397 a.a. *
Waters ×53
* Residue conservation analysis
PDB id:
3l6y
Name: Cell adhesion
Title: Crystal structure of p120 catenin in complex with e-cadherin
Structure: Catenin delta-1. Chain: a, c, e. Fragment: p120 catenin isoform 4a. Synonym: p120 catenin, p120(ctn), cadherin-associated src substrate, cas, p120(cas). Engineered: yes. Mutation: yes. E-cadherin. Chain: b, d, f.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ctnnd1, kiaa0384. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes
Resolution:
3.00Å     R-factor:   0.233     R-free:   0.264
Authors: N.Ishiyama,S.-H.Lee,S.Liu,G.-Y.Li,M.J.Smith,L.F.Reichardt,M.Ikura
Key ref: N.Ishiyama et al. (2010). Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion. Cell, 141, 117-128. PubMed id: 20371349
Date:
27-Dec-09     Release date:   21-Apr-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O60716  (CTND1_HUMAN) -  Catenin delta-1 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		968 a.a.
356 a.a.
Protein chains
Pfam   ArchSchema ?
P12830  (CADH1_HUMAN) -  Cadherin-1 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		882 a.a.
18 a.a.
Protein chain
Pfam   ArchSchema ?
O60716  (CTND1_HUMAN) -  Catenin delta-1 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		968 a.a.
376 a.a.
Protein chain
Pfam   ArchSchema ?
O60716  (CTND1_HUMAN) -  Catenin delta-1 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		968 a.a.
397 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Cell 141:117-128 (2010)
PubMed id: 20371349  
 
 
Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion.
N.Ishiyama, S.H.Lee, S.Liu, G.Y.Li, M.J.Smith, L.F.Reichardt, M.Ikura.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21422226 B.Baum, and M.Georgiou (2011).
Dynamics of adherens junctions in epithelial establishment, maintenance, and remodeling.
  J Cell Biol, 192, 907-917.  
21481789 D.B.Stairs, L.J.Bayne, B.Rhoades, M.E.Vega, T.J.Waldron, J.Kalabis, A.Klein-Szanto, J.S.Lee, J.P.Katz, J.A.Diehl, A.B.Reynolds, R.H.Vonderheide, and A.K.Rustgi (2011).
Deletion of p120-catenin results in a tumor microenvironment with inflammation and cancer that establishes it as a tumor suppressor gene.
  Cancer Cell, 19, 470-483.  
21255999 G.S.Brigidi, and S.X.Bamji (2011).
Cadherin-catenin adhesion complexes at the synapse.
  Curr Opin Neurobiol, 21, 208-214.  
21269602 J.Brasch, O.J.Harrison, G.Ahlsen, S.M.Carnally, R.M.Henderson, B.Honig, and L.Shapiro (2011).
Structure and binding mechanism of vascular endothelial cadherin: a divergent classical cadherin.
  J Mol Biol, 408, 57-73.
PDB code: 3ppe
21358640 J.R.Tollervey, T.Curk, B.Rogelj, M.Briese, M.Cereda, M.Kayikci, J.König, T.Hortobágyi, A.L.Nishimura, V.Zupunski, R.Patani, S.Chandran, G.Rot, B.Zupan, C.E.Shaw, and J.Ule (2011).
Characterizing the RNA targets and position-dependent splicing regulation by TDP-43.
  Nat Neurosci, 14, 452-458.  
21493142 M.C.Nawijn, T.L.Hackett, D.S.Postma, A.J.van Oosterhout, and I.H.Heijink (2011).
E-cadherin: gatekeeper of airway mucosa and allergic sensitization.
  Trends Immunol, 32, 248-255.  
20859058 C.Ozaki, M.Yoshioka, S.Tominaga, Y.Osaka, S.Obata, and S.T.Suzuki (2010).
p120-Catenin is essential for N-cadherin-mediated formation of proper junctional structure, thereby establishing cell polarity in epithelial cells.
  Cell Struct Funct, 35, 81-94.  
20470890 D.Bourboulia, and W.G.Stetler-Stevenson (2010).
Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs): Positive and negative regulators in tumor cell adhesion.
  Semin Cancer Biol, 20, 161-168.  
20715154 Q.Lu (2010).
δ-Catenin dysregulation in cancer: interactions with E-cadherin and beyond.
  J Pathol, 222, 119-123.  
20571587 T.J.Harris, and U.Tepass (2010).
Adherens junctions: from molecules to morphogenesis.
  Nat Rev Mol Cell Biol, 11, 502-514.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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