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J. Biol. Chem., Vol. 282, Issue 52, 37710-37716, December 28, 2007

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Domain Swapping within PDZ2 Is Responsible for Dimerization of ZO Proteins^*

Alan S. Fanning, Ming F. Lye¹, James M. Anderson, and Arnon Lavie²

From the Department of Cell and Molecular Physiology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7545 and the Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois 60607

ZO-1 is a multidomain protein involved in cell-cell junctions and contains three PDZ domains, which are necessary for its function in vivo. PDZ domains play a central role in assembling diverse protein complexes through their ability to recognize short peptide motifs on other proteins. We determined the structure of the second of the three PDZ domains of ZO-1, which is known to promote dimerization as well as bind to C-terminal sequences on connexins. The dimer is stabilized by extensive symmetrical domain swapping of β-strands, which is unlike any other known mechanism of PDZ dimerization. The canonical peptide-binding groove remains intact in both subunits of the PDZ2 dimer and is created by elements contributed from both monomers. This unique structure reveals an additional example of how PDZ domains dimerize and has multiple implications for both peptide binding and oligomerization in vivo.

Received for publication, August 29, 2007 , and in revised form, September 21, 2007.

The atomic coordinates and structure factors (code 2RCZ) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported in part by National Institutes of Health Grant DK61397 and by the Universities of North Carolina and Illinois. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1–S3.

¹ Supported in part by NIDDK Institutional Training Grant T32DK07739, "Training Program in Signal Transduction and Cellular Endocrinology," from the National Institutes of Health.

² To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Genetics, University of Illinois at Chicago, 900 South Ashland Ave., Molecular Biology Research Bldg., Rm. 1108, Chicago, IL 60607. Tel.: 312-355-5029; Fax: 312-355-4535; E-mail: Lavie{at}uic.edu.

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