3b3q

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of a synaptic adhesion complex

Structural highlights

3b3q is a 4 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NLGN1_MOUSE 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. Required to maintain wakefulness quality and normal synchrony of cerebral cortex activity during wakefulness and sleep (PubMed:23716671). The protein is involved in nervous system development.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The heterophilic synaptic adhesion molecules neuroligins and neurexins are essential for establishing and maintaining neuronal circuits by modulating the formation and maturation of synapses. The neuroligin-neurexin adhesion is Ca2+-dependent and regulated by alternative splicing. We report a structure of the complex at a resolution of 2.4 A between the mouse neuroligin-1 (NL1) cholinesterase-like domain and the mouse neurexin-1beta (NX1beta) LNS (laminin, neurexin and sex hormone-binding globulin-like) domain. The structure revealed a delicate neuroligin-neurexin assembly mediated by a hydrophilic, Ca2+-mediated and solvent-supplemented interface, rendering it capable of being modulated by alternative splicing and other regulatory factors. Thermodynamic data supported a mechanism wherein splicing site B of NL1 acts by modulating a salt bridge at the edge of the NL1-NX1beta interface. Mapping neuroligin mutations implicated in autism indicated that most such mutations are structurally destabilizing, supporting deficient neuroligin biosynthesis and processing as a common cause for this brain disorder.

Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions.,Chen X, Liu H, Shim AH, Focia PJ, He X Nat Struct Mol Biol. 2008 Jan;15(1):50-6. Epub 2007 Dec 16. PMID:18084303^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Scheiffele P, Fan J, Choih J, Fetter R, Serafini T. Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons. Cell. 2000 Jun 9;101(6):657-69. PMID:10892652
↑ Graf ER, Zhang X, Jin SX, Linhoff MW, Craig AM. Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins. Cell. 2004 Dec 29;119(7):1013-26. PMID:15620359 doi:10.1016/j.cell.2004.11.035
↑ Varoqueaux F, Aramuni G, Rawson RL, Mohrmann R, Missler M, Gottmann K, Zhang W, Sudhof TC, Brose N. Neuroligins determine synapse maturation and function. Neuron. 2006 Sep 21;51(6):741-54. PMID:16982420 doi:http://dx.doi.org/10.1016/j.neuron.2006.09.003
↑ El Helou J, Bélanger-Nelson E, Freyburger M, Dorsaz S, Curie T, La Spada F, Gaudreault PO, Beaumont É, Pouliot P, Lesage F, Frank MG, Franken P, Mongrain V. Neuroligin-1 links neuronal activity to sleep-wake regulation. Proc Natl Acad Sci U S A. 2013 Jun 11;110(24):9974-9. PMID:23716671 doi:10.1073/pnas.1221381110
↑ Nakanishi M, Nomura J, Ji X, Tamada K, Arai T, Takahashi E, Bućan M, Takumi T. Functional significance of rare neuroligin 1 variants found in autism. PLoS Genet. 2017 Aug 25;13(8):e1006940. PMID:28841651 doi:10.1371/journal.pgen.1006940
↑ Zhang P, Lu H, Peixoto RT, Pines MK, Ge Y, Oku S, Siddiqui TJ, Xie Y, Wu W, Archer-Hartmann S, Yoshida K, Tanaka KF, Aricescu AR, Azadi P, Gordon MD, Sabatini BL, Wong ROL, Craig AM. Heparan Sulfate Organizes Neuronal Synapses through Neurexin Partnerships. Cell. 2018 Sep 6;174(6):1450-1464.e23. PMID:30100184 doi:10.1016/j.cell.2018.07.002
↑ Chen X, Liu H, Shim AH, Focia PJ, He X. Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions. Nat Struct Mol Biol. 2008 Jan;15(1):50-6. Epub 2007 Dec 16. PMID:18084303 doi:10.1038/nsmb1350

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3b3q"

@@ Line 1: / Line 1: @@
 ==Crystal structure of a synaptic adhesion complex==
-<StructureSection load='3b3q' size='340' side='right' caption='[[3b3q]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='3b3q' size='340' side='right'caption='[[3b3q]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3b3q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B3Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3B3Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3b3q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B3Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Nlgn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), NRXN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+<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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b3q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3b3q RCSB], [http://www.ebi.ac.uk/pdbsum/3b3q PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b3q OCA], [https://pdbe.org/3b3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b3q RCSB], [https://www.ebi.ac.uk/pdbsum/3b3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b3q ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/NLGN1_MOUSE NLGN1_MOUSE] 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. Required to maintain wakefulness quality and normal synchrony of cerebral cortex activity during wakefulness and sleep (PubMed:23716671). The protein is involved in nervous system development.<ref>PMID:10892652</ref> <ref>PMID:15620359</ref> <ref>PMID:16982420</ref> <ref>PMID:23716671</ref> <ref>PMID:28841651</ref> <ref>PMID:30100184</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/3b3q_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/3b3q_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=3b3q ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3b3q" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 34: / Line 38: @@
 </StructureSection>
 [[Category: Homo sapiens]]
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Chen, X]]
+[[Category: Chen X]]
-[[Category: Focia, P]]
+[[Category: Focia P]]
-[[Category: He, X]]
+[[Category: He X]]
-[[Category: Liu, H]]
+[[Category: Liu H]]
-[[Category: Shim, A]]
+[[Category: Shim A]]
-[[Category: Adhesion]]
-[[Category: Calcium binding]]
-[[Category: Cell adhesion]]
-[[Category: Heterophilic]]
-[[Category: Membrane]]
-[[Category: Protein-protein complex]]
-[[Category: Synaptic formation]]
-[[Category: Transmembrane]]

3b3q

From Proteopedia

Current revision

Crystal structure of a synaptic adhesion complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox