3BIW

Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex

Summary for 3BIW

• Entry DOI: 10.2210/pdb3biw/pdb
• Related: 3BIX
• Descriptor: Neuroligin-1, Neurexin-1-beta, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: protein-protein complex, esterase domain, lns domain, alpha-beta hydrolase, cell adhesion, cell junction, glycoprotein, membrane, postsynaptic cell membrane, synapse, transmembrane, alternative promoter usage, cell adhesion-cell adhesion complex, cell adhesion/cell adhesion
• Biological source: Rattus norvegicus (Norway rat); More
• Total number of polymer chains: 8
• Total formula weight: 365204.18

Authors

Arac, D.,Boucard, A.A.,Ozkan, E.,Strop, P.,Newell, E.,Sudhof, T.C.,Brunger, A.T. (deposition date: 2007-12-01, release date: 2007-12-18, Last modification date: 2024-10-16)

Primary citation

Arac, D.,Boucard, A.A.,Ozkan, E.,Strop, P.,Newell, E.,Sudhof, T.C.,Brunger, A.T.
Structures of Neuroligin-1 and the Neuroligin-1/Neurexin-1beta Complex Reveal Specific Protein-Protein and Protein-Ca(2+) Interactions.
Neuron, 56:992-1003, 2007

PubMed 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 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: 18093522
DOI: 10.1016/j.neuron.2007.12.002

Experimental method

X-RAY DIFFRACTION (3.5 Å)