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3bix
From Proteopedia
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|PDB= 3bix |SIZE=350|CAPTION= <scene name='initialview01'>3bix</scene>, resolution 1.800Å | |PDB= 3bix |SIZE=350|CAPTION= <scene name='initialview01'>3bix</scene>, resolution 1.800Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Nlgn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= Nlgn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[3biw|3BIW]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bix OCA], [http://www.ebi.ac.uk/pdbsum/3bix PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bix RCSB]</span> | ||
}} | }} | ||
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[[Category: Strop, P.]] | [[Category: Strop, P.]] | ||
[[Category: Sudhof, T C.]] | [[Category: Sudhof, T C.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: NI]] | ||
[[Category: alpha-beta hydrolase]] | [[Category: alpha-beta hydrolase]] | ||
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
| Line 43: | Line 43: | ||
[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:26:47 2008'' |
Revision as of 02:26, 31 March 2008
| |||||||
| , resolution 1.800Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | Nlgn1 (Rattus norvegicus) | ||||||
| Related: | 3BIW
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the extracellular esterase domain of Neuroligin-1
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
3BIX is a Single protein structure of sequence 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 05:26:47 2008
Categories: Rattus norvegicus | Single protein | Arac, D. | Boucard, A A. | Brunger, A T. | Newell, E. | Ozkan, E. | Strop, P. | Sudhof, T C. | Alpha-beta hydrolase | Alternative splicing | Cell adhesion | Cell junction | Esterase domain | Glycoprotein | Membrane | Postsynaptic cell membrane | Synapse | Transmembrane
