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PDBsum entry 3vkf
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Cell adhesion
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PDB id
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3vkf
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Contents |
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560 a.a.
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527 a.a.
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177 a.a.
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References listed in PDB file
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Key reference
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Title
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Higher-Order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin.
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Authors
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H.Tanaka,
N.Miyazaki,
K.Matoba,
T.Nogi,
K.Iwasaki,
J.Takagi.
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Ref.
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Cell Rep, 2012,
2,
101-110.
[DOI no: ]
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PubMed id
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Abstract
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Polymorphic adhesion molecules neurexin and neuroligin (NL) mediate asymmetric
trans-synaptic adhesion, which is crucial for synapse development and function.
It is not known whether or how individual synapse function is controlled by the
interactions between variants and isoforms of these molecules with differing
ectodomain regions. At a physiological concentration of Ca(2+), the ectodomain
complex of neurexin-1 β isoform (Nrx1β) and NL1 spontaneously assembled into
crystals of a lateral sheet-like superstructure topologically compatible with
transcellular adhesion. Correlative light-electron microscopy confirmed
extracellular sheet formation at the junctions between Nrx1β- and
NL1-expressing non-neuronal cells, mimicking the close, parallel synaptic
membrane apposition. The same NL1-expressing cells, however, did not form this
higher-order architecture with cells expressing the much longer neurexin-1 α
isoform, suggesting a functional discrimination mechanism between synaptic
contacts made by different isoforms of neurexin variants.
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