5n7h | pdb_00005n7h

Crystal structure of the coiled-coil domain of human tricellulin

spinqualitylabelsall models 5n7h, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n7h is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease MALD2_HUMAN Autosomal recessive non-syndromic sensorineural deafness type DFNB. The disease is caused by mutations affecting the gene represented in this entry. Function MALD2_HUMAN Plays a role in the formation of the epithelial barriers. The separation of the endolymphatic and perilymphatic spaces of the organ of Corti from one another by epithelial barriers is required for normal hearing. Publication Abstract from PubMed Tricellulin is a tight junction protein localized to tricellular contacts in many epithelial tissues, where it is required for full barrier control. Here, we present crystal structures of the tricellulin C-terminal coiled-coil domain, revealing a potential dimeric arrangement. By combining structural, biochemical, functional, and mutation analyses, we gain insight into the mode of tricellulin oligomerization and suggest a model where dimerization of its cytoplasmic C-terminus may play an auxiliary role in stabilizing homophilic and potentially also heterophilic cis-interactions within tight junctions. Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization.,Schuetz A, Radusheva V, Krug SM, Heinemann U Ann N Y Acad Sci. 2017 Jun 29. doi: 10.1111/nyas.13408. PMID:28661558 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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