5N7H

Crystal structure of the coiled-coil domain of human tricellulin

Summary for 5N7H

Entry DOI	10.2210/pdb5n7h/pdb
Descriptor	MARVEL domain-containing protein 2 (2 entities 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	1
Total formula weight	13977.78
Authors	Schuetz, A.,Heinemann, U. (deposition date: 2017-02-20, release date: 2017-07-12, Last modification date: 2024-05-08)
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation