Structural highlights
DiseaseZO2_HUMAN Defects in TJP2 are involved in familial hypercholanemia (FHCA) [MIM:607748. FHCA is a disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption.[1] FunctionZO2_HUMAN Plays a role in tight junctions and adherens junctions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman 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. Structure of the second PDZ domain from human zonula occludens 2.,Chen H, Tong S, Li X, Wu J, Zhu Z, Niu L, Teng M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Apr 1;65(Pt, 4):327-30. Epub 2009 Mar 25. PMID:19342771[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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