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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2007-12-20
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pubmed:abstractText |
Neurexins and neuroligins provide trans-synaptic connectivity by the Ca2+-dependent interaction of their alternatively spliced extracellular domains. Neuroligins specify synapses in an activity-dependent manner, presumably by binding to neurexins. Here, we present the crystal structures of neuroligin-1 in isolation and in complex with neurexin-1 beta. Neuroligin-1 forms a constitutive dimer, and two neurexin-1 beta monomers bind to two identical surfaces on the opposite faces of the neuroligin-1 dimer to form a heterotetramer. The neuroligin-1/neurexin-1 beta complex exhibits a nanomolar affinity and includes a large binding interface that contains bound Ca2+. Alternatively spliced sites in neurexin-1 beta and in neuroligin-1 are positioned nearby the binding interface, explaining how they regulate the interaction. Structure-based mutations of neuroligin-1 at the interface disrupt binding to neurexin-1 beta, but not the folding of neuroligin-1 and confirm the validity of the binding interface of the neuroligin-1/neurexin-1 beta complex. Our results provide molecular insights for understanding the role of cell-adhesion proteins in synapse function.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0896-6273
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
992-1003
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:18093522-Alternative Splicing,
pubmed-meshheading:18093522-Amino Acid Sequence,
pubmed-meshheading:18093522-Animals,
pubmed-meshheading:18093522-Calcium,
pubmed-meshheading:18093522-Cell Adhesion Molecules, Neuronal,
pubmed-meshheading:18093522-Cells, Cultured,
pubmed-meshheading:18093522-Crystallography,
pubmed-meshheading:18093522-Membrane Proteins,
pubmed-meshheading:18093522-Models, Biological,
pubmed-meshheading:18093522-Models, Molecular,
pubmed-meshheading:18093522-Molecular Sequence Data,
pubmed-meshheading:18093522-Nerve Tissue Proteins,
pubmed-meshheading:18093522-Protein Binding,
pubmed-meshheading:18093522-Protein Conformation,
pubmed-meshheading:18093522-Protein Folding,
pubmed-meshheading:18093522-Rats,
pubmed-meshheading:18093522-Recombinant Proteins,
pubmed-meshheading:18093522-Spectrum Analysis,
pubmed-meshheading:18093522-Surface Plasmon Resonance,
pubmed-meshheading:18093522-Synapses
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pubmed:year |
2007
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pubmed:articleTitle |
Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions.
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pubmed:affiliation |
Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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