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Ann N Y Acad Sci. 2017 Oct;1405(1):147-159. doi: 10.1111/nyas.13408. Epub 2017 Jun 29.

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

Author information

1
Helmholtz Protein Sample Production Facility, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
2
Institute of Clinical Physiology, Campus Benjamin Franklin, Charité - Universitätsmedizin Berlin, Berlin, Germany.
3
Macromolecular Structure and Interaction, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
4
Chemistry and Biochemistry Institute, Freie Universität Berlin, Berlin, Germany.

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:

CC domain; crystal structure; dimerization; tight junction; tricellulin

PMID:
28661558
DOI:
10.1111/nyas.13408
[Indexed for MEDLINE]

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