2RRM

Interplay between phosphatidyl-inositol-phosphates and claudins upon binding to the 1st PDZ domain of zonula occludens 1

Summary for 2RRM

• Entry DOI: 10.2210/pdb2rrm/pdb
• NMR Information: BMRB: 11424
• Descriptor: Tight junction protein ZO-1 (1 entity in total)
• Functional Keywords: pdz domain, protein protein interaction, tight junction protein 1, intercellular adhesion, cell adhesion
• Biological source: Mus musculus (mouse)
• Cellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P39447
• Total number of polymer chains: 1
• Total formula weight: 10817.16

Authors

Hiroaki, H.,Satomura, K.,Goda, N.,Umetsu, Y.,Taniguchi, R.,Ikegami, T.,Furuse, M. (deposition date: 2011-01-06, release date: 2011-05-25, Last modification date: 2024-05-15)

Primary citation

Umetsu, Y.,Goda, N.,Taniguchi, R.,Satomura, K.,Ikegami, T.,Furuse, M.,Hiroaki, H.
1H, 13C, and 15N resonance assignment of the first PDZ domain of mouse ZO-1
Biomol.Nmr Assign., 5:207-210, 2011

PubMed Abstract: Zonula occludens-1 (ZO-1) is a scaffolding molecule critical to the formation of intercellular adhesion structures, such as tight junctions (TJs) and adherens junctions (AJs). ZO-1 contains three PDZ domains followed by a GUK domain and a ZU5 domain. The first PDZ of ZO-1 (ZO-1(PDZ1)) serves as a protein-protein interaction module and interacts with the C-termini of almost all claudins to initiate the formation of a belt-like structure on the lateral membranes, thereby promoting TJ formation. It has been recently reported that approximately 15% of all PDZ domains bind phosphoinositides, and ZO-1(PDZ1) is the one of these. Here we report the (15)N, (13)C, and (1)H chemical shift assignments of the first PDZ domain of mouse ZO-1. The resonance assignments obtained in this work may contribute in clarifying the interplay between the two binary interactions, ZO-1(PDZ1)-claudins and ZO-1(PDZ1)-phospholipids, and suggesting a novel regulation mechanism underlying the formation and maintenance of cell-cell adhesion machinery downstream of the phospholipid signaling pathways.

PubMed: 21431884
DOI: 10.1007/s12104-011-9301-x

Experimental method

SOLUTION NMR