2OSG

Solution Structure and Binding Property of the Domain-swapped Dimer of ZO2PDZ2

Summary for 2OSG

• Entry DOI: 10.2210/pdb2osg/pdb
• Descriptor: Tight junction protein ZO-2 (1 entity in total)
• Functional Keywords: tight junction, zo-2, pdz domain, homodimer, domain swapping, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Cell junction, adherens junction: Q9UDY2
• Total number of polymer chains: 2
• Total formula weight: 18545.68

Authors

Wu, J.W.,Yang, Y.S.,Zhang, J.H.,Ji, P.,Wu, J.H.,Shi, Y.Y. (deposition date: 2007-02-05, release date: 2007-09-25, Last modification date: 2024-05-29)

Primary citation

Wu, J.W.,Yang, Y.S.,Zhang, J.H.,Ji, P.,Du, W.J.,Jiang, P.,Xie, D.H.,Huang, H.D.,Wu, M.,Zhang, G.Z.,Wu, J.H.,Shi, Y.Y.
Domain-swapped Dimerization of the Second PDZ Domain of ZO2 May Provide a Structural Basis for the Polymerization of Claudins
J.Biol.Chem., 282:35988-35999, 2007

PubMed Abstract: Zonula occludens proteins (ZOs), including ZO1/2/3, are tight junction-associated proteins. Each of them contains three PDZ domains. It has been demonstrated that ZO1 can form either homodimers or heterodimers with ZO2 or ZO3 through the second PDZ domain. However, the underlying structural basis is not well understood. In this study, the solution structure of the second PDZ domain of ZO2 (ZO2-PDZ2) was determined using NMR spectroscopy. The results revealed a novel dimerization mode for PDZ domains via three-dimensional domain swapping, which can be generalized to homodimers of ZO1-PDZ2 or ZO3-PDZ2 and heterodimers of ZO1-PDZ2/ZO2-PDZ2 or ZO1-PDZ2/ZO3-PDZ2 due to high conservation between PDZ2 domains in ZO proteins. Furthermore, GST pulldown experiments and immunoprecipitation studies demonstrated that interactions between ZO1-PDZ2 and ZO2-PDZ2 and their self-associations indeed exist both in vitro and in vivo. Chemical cross-linking and dynamic laser light scattering experiments revealed that both ZO1-PDZ2 and ZO2-PDZ2 can form oligomers in solution. This PDZ domain-mediated oligomerization of ZOs may provide a structural basis for the polymerization of claudins, namely the formation of tight junctions.

PubMed: 17897942
DOI: 10.1074/jbc.M703826200

Experimental method

SOLUTION NMR