3bix | pdb_00003bix
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Crystal structure of the extracellular esterase domain of Neuroligin-1
Overview
Neurexins and neuroligins provide trans-synaptic connectivity by the, Ca(2+)-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-1beta. Neuroligin-1 forms a constitutive dimer, and two, neurexin-1beta monomers bind to two identical surfaces on the opposite, faces of the neuroligin-1 dimer to form a heterotetramer. The, neuroligin-1/neurexin-1beta complex exhibits a nanomolar affinity and, includes a large binding interface that contains bound Ca(2+)., Alternatively spliced sites in neurexin-1beta 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-1beta, but not the folding of neuroligin-1 and, confirm the validity of the binding interface of the, neuroligin-1/neurexin-1beta complex. Our results provide molecular, insights for understanding the role of cell-adhesion proteins in synapse, function.
About this Structure
3BIX is a Single protein structure of sequence from Rattus norvegicus with NAG, NI and EDO as ligands. Full crystallographic information is available from OCA.
Reference
Structures of Neuroligin-1 and the Neuroligin-1/Neurexin-1beta Complex Reveal Specific Protein-Protein and Protein-Ca(2+) Interactions., Arac D, Boucard AA, Ozkan E, Strop P, Newell E, Sudhof TC, Brunger AT, Neuron. 2007 Dec 20;56(6):992-1003. PMID:18093522
Page seeded by OCA on Mon Jan 14 18:18:53 2008
