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| {{STRUCTURE_3biw| PDB=3biw | SCENE= }} | | {{STRUCTURE_3biw| PDB=3biw | SCENE= }} |
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| '''Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex'''
| | ===Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18093522}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18093522 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18093522}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Synapse]] | | [[Category: Synapse]] |
| [[Category: Transmembrane]] | | [[Category: Transmembrane]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:49:55 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:45:18 2008'' |