Title : Structures of
neuroligin-1 and the
neuroligin-1 /
neurexin-1 beta complex reveal specific protein-protein and protein-
Ca2 + interactions
Abstract :
- 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 position ed 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
Output (sent_index, trigger,
protein,
sugar,
site):
Output(Part-Of) (sent_index,
protein,
site):
- 4. neuroligin-1 dimer, faces
- 6. neurexin-1 beta, sites
- 6. neuroligin-1, sites
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):