3bix

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|PDB= 3bix |SIZE=350|CAPTION= <scene name='initialview01'>3bix</scene>, resolution 1.800&Aring;
|PDB= 3bix |SIZE=350|CAPTION= <scene name='initialview01'>3bix</scene>, resolution 1.800&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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|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=
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|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.]]
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[[Category: EDO]]
 
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[[Category: NAG]]
 
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[[Category: NI]]
 
[[Category: alpha-beta hydrolase]]
[[Category: alpha-beta hydrolase]]
[[Category: alternative splicing]]
[[Category: alternative splicing]]
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[[Category: transmembrane]]
[[Category: transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:59:23 2008''
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''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

Image:3bix.jpg


PDB ID 3bix

Drag the structure with the mouse to rotate
, 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

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