3L6X: Crystal structure of p120 catenin in complex with E-cadherin

Citation:
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.
PDB ID: 3L6XDownload
MMDB ID: 81568
PDB Deposition Date: 2009/12/27
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 3L6X: dimeric; determined by author and by software (PISA)
Molecular Components in 3L6X
Label Count Molecule
Proteins (2 molecules)
1
Catenin Delta-1(Gene symbol: CTNND1)
Molecule annotation
1
E-cadherin
Molecule annotation
Chemicals (4 molecules)
1
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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