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PDBsum entry 3poy
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Cell adhesion
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PDB id
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3poy
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References listed in PDB file
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Key reference
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Title
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The crystal structure of the α-Neurexin-1 extracellular region reveals a hinge point for mediating synaptic adhesion and function.
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Authors
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M.T.Miller,
M.Mileni,
D.Comoletti,
R.C.Stevens,
M.Harel,
P.Taylor.
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Ref.
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Structure, 2011,
19,
767-778.
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PubMed id
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Abstract
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α- and β-neurexins (NRXNs) are transmembrane cell adhesion proteins that
localize to presynaptic membranes in neurons and interact with the postsynaptic
neuroligins (NLGNs). Their gene mutations are associated with the autism
spectrum disorders. The extracellular region of α-NRXNs, containing nine
independently folded domains, has structural complexity and unique functional
characteristics, distinguishing it from the smaller β-NRXNs. We have solved the
X-ray crystal structure of seven contiguous domains of the α-NRXN-1
extracellular region at 3.0 Å resolution. The structure reveals an arrangement
where the N-terminal five domains adopt a more rigid linear conformation and the
two C-terminal domains form a separate arm connected by a flexible hinge. In an
extended conformation the molecule is suitably configured to accommodate a bound
NLGN molecule, as supported by structural comparison and surface plasmon
resonance. These studies provide the structural basis for a multifunctional
synaptic adhesion complex mediated by α-NRXN-1.
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