Open AccessStructure of the second PDZ domain from human zonula occludens 2
Author(s) -
Chen Hui,
Tong Shuilong,
Li Xu,
Wu Jiawen,
Zhu Zhiqiang,
Niu Liwen,
Teng Maikun
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109002334
Subject(s) - pdz domain , dimer , protein subunit , domain (mathematical analysis) , crystallography , biophysics , chemistry , biology , microbiology and biotechnology , biochemistry , gene , mathematics , mathematical analysis , organic chemistry
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 Å resolution, revealing a dimer in the asymmetric unit. The dimer is stabilized by extensive symmetrical domain‐swapping of the β1 and β2 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.