3E17

Crystal structure of the second PDZ domain from human Zona Occludens-2

Summary for 3E17

• Entry DOI: 10.2210/pdb3e17/pdb
• Descriptor: Tight junction protein ZO-2 (2 entities in total)
• Functional Keywords: domain swapping, alternative promoter usage, alternative splicing, cell junction, cell membrane, disease mutation, membrane, nucleus, phosphoprotein, polymorphism, sh3 domain, tight junction, cell adhesion
• Biological source: Homo sapiens (Human)
• Cellular location: Cell junction, adherens junction: Q9UDY2
• Total number of polymer chains: 2
• Total formula weight: 20029.29

Authors

Chen, H.,Tong, S.L.,Teng, M.K.,Niu, L.W. (deposition date: 2008-08-01, release date: 2009-07-21, Last modification date: 2023-11-01)

Primary citation

Chen, H.,Tong, S.,Li, X.,Wu, J.,Zhu, Z.,Niu, L.,Teng, M.
Structure of the second PDZ domain from human zonula occludens 2
Acta Crystallogr.,Sect.F, 65:327-330, 2009

PubMed 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.

PubMed: 19342771
DOI: 10.1107/S1744309109002334

Experimental method

X-RAY DIFFRACTION (1.75 Å)