Structural Features of Tight-Junction Proteins
作者： Udo Heinemann , Anja Schuetz
DOI: 10.3390/IJMS20236020
关键词:
摘要: Tight junctions are complex supramolecular entities composed of integral membrane proteins, membrane-associated and soluble cytoplasmic proteins engaging in an intricate dynamic system protein-protein interactions. Three-dimensional structures several tight-junction or their isolated domains have been determined by X-ray crystallography, nuclear magnetic resonance spectroscopy, cryo-electron microscopy. These provide direct insight into molecular interactions that contribute to the formation, integrity, function tight junctions. In addition, known experimental allowed modeling ligand-binding events involving proteins. Here, we review published We show these a limited set structural motifs highlight common types between ligands motifs.
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G. Krause, J. Protze, J. Piontek, Assembly and function of claudins: Structure–function relationships based on homology models and crystal structures Seminars in Cell & Developmental Biology. ,vol. 42, pp. 3- 12 ,(2015) , 10.1016/J.SEMCDB.2015.04.010
Dorothee Günzel, Michael Fromm, Claudins and other tight junction proteins. Comprehensive Physiology. ,vol. 2, pp. 1819- 1852 ,(2012) , 10.1002/CPHY.C110045
Liron Elkouby-Naor, Tamar Ben-Yosef, Functions of claudin tight junction proteins and their complex interactions in various physiological systems. International Review of Cell and Molecular Biology. ,vol. 279, pp. 1- 32 ,(2010) , 10.1016/S1937-6448(10)79001-8
Vladimir N. Uversky, What does it mean to be natively unfolded? European Journal of Biochemistry. ,vol. 269, pp. 2- 12 ,(2002) , 10.1046/J.0014-2956.2001.02649.X
Klaas E. A. Max, Markus Zeeb, Ralf Bienert, Jochen Balbach, Udo Heinemann, Common mode of DNA binding to cold shock domains. Crystal structure of hexathymidine bound to the domain-swapped form of a major cold shock protein from Bacillus caldolyticus. FEBS Journal. ,vol. 274, pp. 1265- 1279 ,(2007) , 10.1111/J.1742-4658.2007.05672.X
L. A. Staehelin, Further Observations on the Fine Structure of Freeze-Cleaved Tight Junctions Journal of Cell Science. ,vol. 13, pp. 763- 786 ,(1973) , 10.1242/JCS.13.3.763
H. Bauer, J. Zweimueller-Mayer, P. Steinbacher, A. Lametschwandtner, H. C. Bauer, The Dual Role of Zonula Occludens (ZO) Proteins BioMed Research International. ,vol. 2010, pp. 402593- 402593 ,(2010) , 10.1155/2010/402593
Hermann Schindelin, Mohamed A. Marahiel, Udo Heinemann, Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature. ,vol. 364, pp. 164- 168 ,(1993) , 10.1038/364164A0
J. K. Walter, V. Castro, M. Voss, K. Gast, C. Rueckert, J. Piontek, Ingolf E. Blasig, Redox-sensitivity of the dimerization of occludin Cellular and Molecular Life Sciences. ,vol. 66, pp. 3655- 3662 ,(2009) , 10.1007/S00018-009-0150-Z
Youjun Li, Zhiyi Wei, Yan Yan, Qingwen Wan, Quansheng Du, Mingjie Zhang, Structure of Crumbs tail in complex with the PALS1 PDZ-SH3-GK tandem reveals a highly specific assembly mechanism for the apical Crumbs complex. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 111, pp. 17444- 17449 ,(2014) , 10.1073/PNAS.1416515111