Structure of the second PDZ domain from human zonula occludens 2.

Hui Chen, Shuilong Tong, Xu Li, Jiawen Wu, Zhiqiang Zhu, Liwen Niu, Maikun Teng

Acta crystallographica. Section F, Structural biology and crystallization communications 2009 Apr 01

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Human zonula occludens 2 (ZO-2) protein is a multi-domain protein that consists of an SH3 domain, a GK domain and three copies of a PDZ domain with slight divergence. The three PDZ domains act as protein-recognition modules that may mediate protein assembly and subunit localization. The crystal structure of the second PDZ domain of ZO-2 (ZO-2 PDZ2) was determined by molecular replacement at 1.75 A resolution, revealing a dimer in the asymmetric unit. The dimer is stabilized by extensive symmetrical domain-swapping of the beta1 and beta2 strands. Structural comparison shows that the ZO-2 PDZ2 homodimer may have a similar ligand-binding pattern to the ZO-1 PDZ2-connexin 43 complex.

Citation

Hui Chen, Shuilong Tong, Xu Li, Jiawen Wu, Zhiqiang Zhu, Liwen Niu, Maikun Teng. Structure of the second PDZ domain from human zonula occludens 2. Acta crystallographica. Section F, Structural biology and crystallization communications. 2009 Apr 01;65(Pt 4):327-30