3biw
From Proteopedia
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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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[[Category: Strop, P.]] | [[Category: Strop, P.]] | ||
[[Category: Sudhof, T C.]] | [[Category: Sudhof, T C.]] | ||
| - | [[Category: | + | [[Category: Alpha-beta hydrolase]] |
| - | [[Category: | + | [[Category: Alternative promoter usage]] |
| - | [[Category: | + | [[Category: Alternative splicing]] |
| - | [[Category: | + | [[Category: Cell adhesion]] |
| - | [[Category: | + | [[Category: Cell adhesion/cell adhesion complex]] |
| - | [[Category: | + | [[Category: Cell junction]] |
| - | [[Category: | + | [[Category: Esterase domain]] |
| - | [[Category: | + | [[Category: Glycoprotein]] |
| - | [[Category: | + | [[Category: Lns domain]] |
| - | [[Category: | + | [[Category: Membrane]] |
| - | [[Category: | + | [[Category: Postsynaptic cell membrane]] |
| - | [[Category: | + | [[Category: Protein-protein complex]] |
| - | [[Category: | + | [[Category: Synapse]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 17:49, 4 May 2008
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 Sun May 4 20:49:55 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
