Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization.

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Item Type:	Article
Title:	Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization.
Creators Name:	Schuetz, A., Radusheva, V., Krug, S.M. and Heinemann, U.
Abstract:	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.
Keywords:	Tight Junction, Tricellulin, Crystal Structure, CC Domain, Dimerization
Source:	Annals of the New York Academy of Sciences
ISSN:	0077-8923
Publisher:	New York Academy of Sciences
Volume:	1405
Number:	1
Page Range:	147-159
Date:	October 2017
Official Publication:	https://doi.org/10.1111/nyas.13408
PubMed:	View item in PubMed

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