Domain swapping within PDZ2 is responsible for dimerization of ZO proteins.

@article{Fanning2007DomainSW,
  title={Domain swapping within PDZ2 is responsible for dimerization of ZO proteins.},
  author={Alan S. Fanning and Ming F Lye and James Melvin Anderson and Arnon Lavie},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 52},
  pages={37710-6}
}
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… CONTINUE READING

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