3biw
From Proteopedia
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- | [[Image:3biw.jpg|left|200px]] | + | [[Image:3biw.jpg|left|200px]] |
- | + | ||
- | '''Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex''' | + | {{Structure |
+ | |PDB= 3biw |SIZE=350|CAPTION= <scene name='initialview01'>3biw</scene>, resolution 3.500Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= Nlgn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]), Nrxn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 3BIW is a [ | + | 3BIW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BIW OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18093522 18093522] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:59:20 2008'' |
Revision as of 16:59, 20 March 2008
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, resolution 3.500Å | |||||||
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Ligands: | and | ||||||
Gene: | Nlgn1 (Rattus norvegicus), Nrxn1 (Rattus norvegicus) | ||||||
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 Thu Mar 20 18:59:20 2008
Categories: Protein complex | Rattus norvegicus | Arac, D. | Boucard, A A. | Brunger, A T. | Newell, E. | Ozkan, E. | Strop, P. | Sudhof, T C. | CA | NAG | 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