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Structural features of tight-junction proteins

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Item Type:Review
Title:Structural features of tight-junction proteins
Creators Name:Heinemann, U. and Schuetz, A.
Abstract:Tight junctions are complex supramolecular entities composed of integral membrane proteins, membrane-associated and soluble cytoplasmic proteins engaging in an intricate and dynamic system of protein-protein interactions. Three-dimensional structures of several tight-junction proteins or their isolated domains have been determined by X-ray crystallography, nuclear magnetic resonance spectroscopy, and cryo-electron microscopy. These structures provide direct insight into molecular interactions that contribute to the formation, integrity, or function of tight junctions. In addition, the known experimental structures have allowed the modeling of ligand-binding events involving tight-junction proteins. Here, we review the published structures of tight-junction proteins. We show that these proteins are composed of a limited set of structural motifs and highlight common types of interactions between tight-junction proteins and their ligands involving these motifs.
Keywords:Tight Junction, Protein Structure, Protein Domain, Claudins, Occludin, Tricellulin, Junctional Adhesion Molecule, Zonula Occludens, MAGUK Proteins, PDZ Domain, Animals
Source:International Journal of Molecular Sciences
ISSN:1422-0067
Publisher:MDPI
Volume:20
Number:23
Page Range:6020
Date:29 November 2019
Official Publication:https://doi.org/10.3390/ijms20236020
PubMed:View item in PubMed

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