title: Structure of the second PDZ domain from human zonula occludens 2.
abstract: 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.
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
authors.forename: Hui
authors.initials: H
authors.lastname: Chen
authors.forename: Shuilong
authors.initials: S
authors.lastname: Tong
authors.forename: Xu
authors.initials: X
authors.lastname: Li
authors.forename: Jiawen
authors.initials: J
authors.lastname: Wu
authors.forename: Zhiqiang
authors.initials: Z
authors.lastname: Zhu
authors.forename: Liwen
authors.initials: L
authors.lastname: Niu
authors.forename: Maikun
authors.initials: M
authors.lastname: Teng