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PDBsum entry 5ayq
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Metal transport
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PDB id
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5ayq
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References listed in PDB file
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Key reference
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Title
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Structure-Based site-Directed photo-Crosslinking analyses of multimeric cell-Adhesive interactions of voltage-Gated sodium channel β subunits.
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Authors
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H.Shimizu,
H.Miyazaki,
N.Ohsawa,
S.Shoji,
Y.Ishizuka-Katsura,
A.Tosaki,
F.Oyama,
T.Terada,
K.Sakamoto,
M.Shirouzu,
S.Sekine,
N.Nukina,
S.Yokoyama.
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Ref.
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Sci Rep, 2016,
6,
26618.
[DOI no: ]
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PubMed id
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Abstract
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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.
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