5N7I

Crystal structure of the coiled-coil domain of human tricellulin

Summary for 5N7I

• Entry DOI: 10.2210/pdb5n7i/pdb
• Descriptor: MARVEL domain-containing protein 2 (1 entity in total)
• Functional Keywords: tight junction, cc domain, dimerization, cell adhesion
• Biological source: Homo sapiens (Human)
• Cellular location: Cell membrane; Multi-pass membrane protein: Q8N4S9
• Total number of polymer chains: 2
• Total formula weight: 27611.10

Authors

Schuetz, A.,Heinemann, U. (deposition date: 2017-02-20, release date: 2017-07-12, Last modification date: 2024-01-17)

Primary citation

Schuetz, A.,Radusheva, V.,Krug, S.M.,Heinemann, U.
Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization.
Ann. N. Y. Acad. Sci., 1405:147-159, 2017

PubMed 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.

PubMed: 28661558
DOI: 10.1111/nyas.13408

Experimental method

X-RAY DIFFRACTION (2.88 Å)