3L6Y
Crystal structure of p120 catenin in complex with E-cadherin
Summary for 3L6Y
Entry DOI | 10.2210/pdb3l6y/pdb |
Related | 3L6X |
Descriptor | Catenin delta-1, E-cadherin (3 entities in total) |
Functional Keywords | p120, catenin, cadherin, e-cadherin, armadillo, arm, jmd, cell adhesion, complex, cell-cell adhesion, arvcf, delta-catenin, p0071, dp120, jac-1, cell membrane, membrane, nucleus, phosphoprotein, transcription, transcription regulation, wnt signaling pathway |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm . Isoform 1A: Nucleus . Isoform 2A: Nucleus . Isoform 3A: Nucleus : O60716 |
Total number of polymer chains | 6 |
Total formula weight | 202109.79 |
Authors | Ishiyama, N.,Lee, S.-H.,Liu, S.,Li, G.-Y.,Smith, M.J.,Reichardt, L.F.,Ikura, M. (deposition date: 2009-12-27, release date: 2010-04-21, Last modification date: 2023-09-06) |
Primary citation | Ishiyama, N.,Lee, S.H.,Liu, S.,Li, G.Y.,Smith, M.J.,Reichardt, L.F.,Ikura, M. Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion. Cell(Cambridge,Mass.), 141:117-128, 2010 Cited by PubMed 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. PubMed: 20371349DOI: 10.1016/j.cell.2010.01.017 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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