PDBsum entry 3tsz

Cell adhesion

PDB id: 3tsz

Contents

Protein chain

341 a.a.

Ligands

GLU-PHE-LYS-GLN-THR-SER-SER-PHE-LEU-VAL

Waters ×40

PDB id:

3tsz

Name:

Cell adhesion

Title:

Crystal structure of pdz3-sh3-guk core module from human zo-1 in complex with 12mer peptide from human jam-a cytoplasmic tail

Structure:

Tight junction protein zo-1. Chain: a. Fragment: pdz3-sh3-guk (unp residues 417-803). Synonym: tight junction protein 1, zona occludens protein 1, zonula occludens protein 1. Engineered: yes. Junctional adhesion molecule a. Chain: b. Fragment: jam-a_p12 (unp residues 288-299).

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: tjp1, zo1. Expressed in: escherichia coli. Expression_system_taxid: 511693. Synthetic: yes. Other_details: synthetic peptide

Resolution:

2.50Å R-factor: 0.247 R-free: 0.309

Authors:

J.Nomme,A.Lavie

Key ref:

J.Nomme et al. (2011). The Src homology 3 domain is required for junctional adhesion molecule binding to the third PDZ domain of the scaffolding protein ZO-1. J Biol Chem, 286, 43352-43360. PubMed id: 22030391 DOI: 10.1074/jbc.M111.304089

Date:

13-Sep-11 Release date: 12-Oct-11

Protein chain

Q07157  (ZO1_HUMAN) -  Tight junction protein ZO-1 from Homo sapiens

Seq: 1748 a.a.

Struc: 341 a.a.

DOI no: 10.1074/jbc.M111.304089

J Biol Chem 286:43352-43360 (2011)

PubMed id: 22030391

The Src homology 3 domain is required for junctional adhesion molecule binding to the third PDZ domain of the scaffolding protein ZO-1.

J.Nomme, A.S.Fanning, M.Caffrey, M.F.Lye, J.M.Anderson, A.Lavie.

ABSTRACT

Tight junctions are cell-cell contacts that regulate the paracellular flux of solutes and prevent pathogen entry across cell layers. The assembly and permeability of this barrier are dependent on the zonula occludens (ZO) membrane-associated guanylate kinase (MAGUK) proteins ZO-1, -2, and -3. MAGUK proteins are characterized by a core motif of protein-binding domains that include a PDZ domain, a Src homology 3 (SH3) domain, and a region of homology to guanylate kinase (GUK); the structure of this core motif has never been determined for any MAGUK. To better understand how ZO proteins organize the assembly of protein complexes we have crystallized the entire PDZ3-SH3-GUK core motif of ZO-1. We have also crystallized this core motif in complex with the cytoplasmic tail of the ZO-1 PDZ3 ligand, junctional adhesion molecule A (JAM-A) to determine how the activity of different domains is coordinated. Our study shows a new feature for PDZ class II ligand binding that implicates the two highly conserved Phe(-2) and Ser(-3) residues of JAM. Our x-ray structures and NMR experiments also show for the first time a role for adjacent domains in the binding of ligands to PDZ domains in the MAGUK proteins family.