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

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.

Pubmed ID: 18093522


  • Araç D
  • Boucard AA
  • Ozkan E
  • Strop P
  • Newell E
  • Südhof TC
  • Brunger AT



Publication Data

December 20, 2007

Associated Grants

  • Agency: NIMH NIH HHS, Id: R37 MH52804-08

Mesh Terms

  • Alternative Splicing
  • Amino Acid Sequence
  • Animals
  • Calcium
  • Cell Adhesion Molecules, Neuronal
  • Cells, Cultured
  • Crystallography
  • Membrane Proteins
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Nerve Tissue Proteins
  • Protein Binding
  • Protein Conformation
  • Protein Folding
  • Rats
  • Recombinant Proteins
  • Spectrum Analysis
  • Surface Plasmon Resonance
  • Synapses