3biw
From Proteopedia
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| , resolution 3.500Å | |||||||
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| Ligands: | , | ||||||
| Gene: | Nlgn1 (Rattus norvegicus), Nrxn1 (Rattus norvegicus) | ||||||
| Related: | 3BIX
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex
Overview
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.
About this Structure
3BIW is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ 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 Mar 31 05:26:45 2008
Categories: Protein complex | Rattus norvegicus | Arac, D. | Boucard, A A. | Brunger, A T. | Newell, E. | Ozkan, E. | Strop, P. | Sudhof, T C. | Alpha-beta hydrolase | Alternative promoter usage | Alternative splicing | Cell adhesion | Cell adhesion/cell adhesion complex | Cell junction | Esterase domain | Glycoprotein | Lns domain | Membrane | Postsynaptic cell membrane | Protein-protein complex | Synapse | Transmembrane
