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Crystal structure of the tricellulin C‐terminal coiled‐coil domain reveals a unique mode of dimerization
Author(s) -
Schuetz Anja,
Radusheva Veselina,
Krug Susanne M.,
Heinemann Udo
Publication year - 2017
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/nyas.13408
Subject(s) - coiled coil , domain (mathematical analysis) , cytoplasm , terminal (telecommunication) , c terminus , chemistry , tight junction , protein structure , protein domain , crystal structure , fold (higher order function) , crystallography , biophysics , biology , biochemistry , amino acid , computer science , gene , mathematical analysis , telecommunications , mathematics , programming language
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.