5v5w

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m (Protected "5v5w" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5v5w is ON HOLD
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==Molecular Mechanism of MDGA1: Regulation of Neuroligin 2:Neurexin Trans-synaptic Bridges==
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<StructureSection load='5v5w' size='340' side='right' caption='[[5v5w]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5v5w]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V5W FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5v5v|5v5v]]</td></tr>
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<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=5v5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v5w OCA], [http://pdbe.org/5v5w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v5w RCSB], [http://www.ebi.ac.uk/pdbsum/5v5w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v5w ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/MDGA1_HUMAN MDGA1_HUMAN]] Required for radial migration of cortical neurons in the superficial layer of the neocortex (By similarity). Plays a role in the formation or maintenance of inhibitory synapses. May function by inhibiting the activity of NLGN2.<ref>PMID:23248271</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Neuroligins and neurexins promote synapse development and validation by forming trans-synaptic bridges spanning the synaptic cleft. Select pairs promote excitatory and inhibitory synapses, with neuroligin 2 (NLGN2) limited to inhibitory synapses and neuroligin 1 (NLGN1) dominating at excitatory synapses. The cell-surface molecules, MAM domain-containing glycosylphosphatidylinositol anchor 1 (MDGA1) and 2 (MDGA2), regulate trans-synaptic adhesion between neurexins and neuroligins, impacting NLGN2 and NLGN1, respectively. We have determined the molecular mechanism of MDGA action. MDGA1 Ig1-Ig2 is sufficient to bind NLGN2 with nanomolar affinity; its crystal structure reveals an unusual locked rod-shaped array. In the crystal structure of the complex, two MDGA1 Ig1-Ig2 molecules each span the entire NLGN2 dimer. Site-directed mutagenesis confirms the observed interaction interface. Strikingly, Ig1 from MDGA1 binds to the same region on NLGN2 as neurexins do. Thus, MDGAs regulate the formation of neuroligin-neurexin trans-synaptic bridges by sterically blocking access of neurexins to neuroligins.
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Authors:
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Molecular Mechanism of MDGA1: Regulation of Neuroligin 2:Neurexin Trans-synaptic Bridges.,Gangwar SP, Zhong X, Seshadrinathan S, Chen H, Machius M, Rudenko G Neuron. 2017 Jun 21;94(6):1132-1141.e4. doi: 10.1016/j.neuron.2017.06.009. PMID:28641112<ref>PMID:28641112</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5v5w" style="background-color:#fffaf0;"></div>
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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: Gangwar, S P]]
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[[Category: Machius, M]]
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[[Category: Rudenko, G]]
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[[Category: Cell adhesion]]
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[[Category: Mdga]]
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[[Category: Regulatory molecule]]
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[[Category: Synaptic organizer]]

Revision as of 10:03, 27 September 2017

Molecular Mechanism of MDGA1: Regulation of Neuroligin 2:Neurexin Trans-synaptic Bridges

5v5w, resolution 2.72Å

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