2osg

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

Overview

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.

About this Structure

2OSG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Domain-swapped Dimerization of the Second PDZ Domain of ZO2 May Provide a Structural Basis for the Polymerization of Claudins., Wu J, Yang Y, Zhang J, Ji P, Du W, Jiang P, Xie D, Huang H, Wu M, Zhang G, Wu J, Shi Y, J Biol Chem. 2007 Dec 7;282(49):35988-35999. Epub 2007 Sep 25. PMID:17897942

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