Structural Features of Tight-Junction Proteins.

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ID: 97981
2019
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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.
Reference Key
heinemann2019structuralinternational Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Heinemann, Udo;Schuetz, Anja;
Journal International journal of molecular sciences
Year 2019
DOI
E6020
URL
Keywords
protein structure tight junction occludin tricellulin maguk proteins pdz domain claudins junctional adhesion molecule protein domain zonula occludens

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