3biw

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[[Image:3biw.jpg|left|200px]]
 
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==Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex==
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The line below this paragraph, containing "STRUCTURE_3biw", creates the "Structure Box" on the page.
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<StructureSection load='3biw' size='340' side='right'caption='[[3biw]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3biw]] is a 8 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BIW FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_3biw| PDB=3biw | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3biw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3biw OCA], [https://pdbe.org/3biw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3biw RCSB], [https://www.ebi.ac.uk/pdbsum/3biw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3biw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NLGN1_RAT NLGN1_RAT] Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses.<ref>PMID:9325340</ref> <ref>PMID:15620359</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bi/3biw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3biw ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex'''
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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<ref>PMID:18093522</ref>
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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].
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</div>
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<div class="pdbe-citations 3biw" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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]
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*[[Neurexin|Neurexin]]
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[[Category: Protein complex]]
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*[[Neuroligin|Neuroligin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Arac, D.]]
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[[Category: Arac D]]
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[[Category: Boucard, A A.]]
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[[Category: Boucard AA]]
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[[Category: Brunger, A T.]]
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[[Category: Brunger AT]]
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[[Category: Newell, E.]]
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[[Category: Newell E]]
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[[Category: Ozkan, E.]]
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[[Category: Ozkan E]]
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[[Category: Strop, P.]]
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[[Category: Strop P]]
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[[Category: Sudhof, T C.]]
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[[Category: Sudhof TC]]
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[[Category: Alpha-beta hydrolase]]
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[[Category: Alternative promoter usage]]
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[[Category: Alternative splicing]]
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[[Category: Cell adhesion]]
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[[Category: Cell adhesion/cell adhesion complex]]
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[[Category: Cell junction]]
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[[Category: Esterase domain]]
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[[Category: Glycoprotein]]
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[[Category: Lns domain]]
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[[Category: Membrane]]
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[[Category: Postsynaptic cell membrane]]
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[[Category: Protein-protein complex]]
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[[Category: Synapse]]
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[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:49:55 2008''
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Current revision

Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex

PDB ID 3biw

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