5AYQ

Structure-based site-directed photo-crosslinking analyses of multimeric cell-adhesive interactions of VGSC beta subunits

Summary for 5AYQ

• Entry DOI: 10.2210/pdb5ayq/pdb
• Descriptor: Sodium channel subunit beta-4 (2 entities in total)
• Functional Keywords: sodium channel beta subunit, metal transport
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 2
• Total formula weight: 30592.08

Authors

Shimizu, H. (deposition date: 2015-09-01, release date: 2016-06-08, Last modification date: 2024-11-20)

Primary citation

Shimizu, H.,Miyazaki, H.,Ohsawa, N.,Shoji, S.,Ishizuka-Katsura, Y.,Tosaki, A.,Oyama, F.,Terada, T.,Sakamoto, K.,Shirouzu, M.,Sekine, S.,Nukina, N.,Yokoyama, S.
Structure-based site-directed photo-crosslinking analyses of multimeric cell-adhesive interactions of voltage-gated sodium channel beta subunits
Sci Rep, 6:26618-26618, 2016

PubMed Abstract: The β1, β2, and β4 subunits of voltage-gated sodium channels reportedly function as cell adhesion molecules. The present crystallographic analysis of the β4 extracellular domain revealed an antiparallel arrangement of the β4 molecules in the crystal lattice. The interface between the two antiparallel β4 molecules is asymmetric, and results in a multimeric assembly. Structure-based mutagenesis and site-directed photo-crosslinking analyses of the β4-mediated cell-cell adhesion revealed that the interface between the antiparallel β4 molecules corresponds to that in the trans homophilic interaction for the multimeric assembly of β4 in cell-cell adhesion. This trans interaction mode is also employed in the β1-mediated cell-cell adhesion. Moreover, the β1 gene mutations associated with generalized epilepsy with febrile seizures plus (GEFS+) impaired the β1-mediated cell-cell adhesion, which should underlie the GEFS+ pathogenesis. Thus, the structural basis for the β-subunit-mediated cell-cell adhesion has been established.

PubMed: 27216889
DOI: 10.1038/srep26618

Experimental method

X-RAY DIFFRACTION (1.7 Å)