PDBsum entry 4oeo

Cell adhesion

PDB id: 4oeo

Contents

Protein chains

94 a.a.

Ligands

ACT ×3

SO4 ×2

12P ×2

Waters ×96

PDB id:

4oeo

Name:

Cell adhesion

Title:

High resolution crystal structure of the unliganded zo-1 pdz1 domain

Structure:

Tight junction protein zo-1. Chain: a, b, c. Fragment: pdz1 domain, unp residues 18-110. Synonym: tight junction protein 1, zona occludens protein 1, zonula occludens protein 1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: tjp1, zo1. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.90Å R-factor: 0.198 R-free: 0.243

Authors:

J.Nomme,A.Lavie

Key ref:

J.Nomme et al. (2015). Structural Basis of a Key Factor Regulating the Affinity between the Zonula Occludens First PDZ Domain and Claudins. J Biol Chem, 290, 16595-16606. PubMed id: 26023235 DOI: 10.1074/jbc.M115.646695

Date:

13-Jan-14 Release date: 14-Jan-15

Protein chains

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

Seq: 1748 a.a.

Struc: 94 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1074/jbc.M115.646695

J Biol Chem 290:16595-16606 (2015)

PubMed id: 26023235

Structural Basis of a Key Factor Regulating the Affinity between the Zonula Occludens First PDZ Domain and Claudins.

J.Nomme, A.Antanasijevic, M.Caffrey, C.M.Van Itallie, J.M.Anderson, A.S.Fanning, A.Lavie.

ABSTRACT

The molecular seal between epithelial cells, called the tight junction (TJ), is built by several membrane proteins, with claudins playing the most prominent role. The scaffold proteins of the zonula occludens family are required for the correct localization of claudins and hence formation of the TJ. The intracellular C terminus of claudins binds to the N-terminal PDZ domain of zonula occludens proteins (PDZ1). Of the 23 identified human claudin proteins, nine possess a tyrosine at the -6 position. Here we show that the claudin affinity for PDZ1 is dependent on the presence or absence of this tyrosine and that the affinity is reduced if the tyrosine is modified by phosphorylation. The PDZ1 β2-β3 loop undergoes a significant conformational change to accommodate this tyrosine. Cell culture experiments support a regulatory role for this tyrosine. Plasticity has been recognized as a critical property of TJs that allow cell remodeling and migration. Our work provides a molecular framework for how TJ plasticity may be regulated.