RGD Reference Report - Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions. - Rat Genome Database

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Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions.

Authors: Arac, D  Boucard, AA  Ozkan, E  Strop, P  Newell, E  Sudhof, TC  Brunger, AT 
Citation: Arac D, etal., Neuron. 2007 Dec 20;56(6):992-1003.
RGD ID: 2314457
Pubmed: PMID:18093522   (View Abstract at PubMed)
DOI: DOI:10.1016/j.neuron.2007.12.002   (Journal Full-text)

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.



Gene Ontology Annotations    Click to see Annotation Detail View

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Nlgn1Ratprotein complex involved in cell-cell adhesion part_ofIPI PMID:18093522ComplexPortal 
Nrxn1Ratprotein complex involved in cell-cell adhesion part_ofIPI PMID:18093522ComplexPortal 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Nlgn1Ratneurexin family protein binding  IPINrxn1 (Rattus norvegicus) RGD 
Nrxn1Ratprotein binding  IPINlgn1 (Rattus norvegicus) RGD 
Nlgn1Ratprotein-containing complex binding  IDA heterotetramerization with Nrxn1RGD 
Nrxn1Ratprotein-containing complex binding  IDA heterotetramerization with Nlgn1RGD 

Objects Annotated

Genes (Rattus norvegicus)
Nlgn1  (neuroligin 1)
Nrxn1  (neurexin 1)


Additional Information