<StructureSection load='3b3q' size='350' side='right' scene='' caption='Dimer of two mouse neuroligin-1 cholinesterase-like domains (grey and green) in complex with two neurexin-beta1 LNS6 domains (pink and cyan) and Ca+2 ions (green) [[3b3q]]'>
[[Image:3be8a.png|left|200px|thumb|Crystal Structure of human Neuroligin [[3be8]]]]
[[Image:3be8a.png|left|200px|thumb|Crystal Structure of human Neuroligin [[3be8]]]]
{{STRUCTURE_3b3q| PDB=3b3q | SIZE=350| SCENE= |right|CAPTION=Dimer of two mouse neuroligin-1 cholinesterase-like domains (grey and green) in complex with two neurexin-beta1 LNS6 domains (pink and cyan) and Ca+2 ions (green) [[3b3q]] }}
== Function ==
== Function ==
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== Structural insights ==
== Structural insights ==
The NLGN-NRXN complex involves the octahedrally coordinated Ca+2 ion<ref>PMID:18084303</ref>.
The NLGN-NRXN complex involves the octahedrally coordinated Ca+2 ion<ref>PMID:18084303</ref>.
</StructureSection>
== 3D Structures of Neuroligin ==
== 3D Structures of Neuroligin ==
Revision as of 07:43, 15 May 2016
Dimer of two mouse neuroligin-1 cholinesterase-like domains (grey and green) in complex with two neurexin-beta1 LNS6 domains (pink and cyan) and Ca+2 ions (green) 3b3q
Neuroligins (NLGN) are a family of postsynaptic proteins which bind to the presynaptic Neurexin (NRXN) to form a complex which attaches neurons. In humans the NLGN family contains 4 to 5 members that are numbered 1, 2, 3, 4X and 5 or 4Y[1].
NLGN-4 is localized to glyceric post-synapses and regulates retina inhibition[4].
Disease
Mutations in NLGN 4 are associated with autism and mental retardation[5].
Structural insights
The NLGN-NRXN complex involves the octahedrally coordinated Ca+2 ion[6].
↑Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P. Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion. Neuron. 2007 Dec 20;56(6):979-91. PMID:18093521 doi:10.1016/j.neuron.2007.11.013
↑Liu A, Zhou Z, Dang R, Zhu Y, Qi J, He G, Leung C, Pak D, Jia Z, Xie W. Neuroligin 1 regulates spines and synaptic plasticity via LIMK1/cofilin-mediated actin reorganization. J Cell Biol. 2016 Feb 15;212(4):449-63. doi: 10.1083/jcb.201509023. PMID:26880202 doi:https://dx.doi.org/10.1083/jcb.201509023
↑Hoon M, Soykan T, Falkenburger B, Hammer M, Patrizi A, Schmidt KF, Sassoe-Pognetto M, Lowel S, Moser T, Taschenberger H, Brose N, Varoqueaux F. Neuroligin-4 is localized to glycinergic postsynapses and regulates inhibition in the retina. Proc Natl Acad Sci U S A. 2011 Feb 15;108(7):3053-8. doi:, 10.1073/pnas.1006946108. Epub 2011 Jan 31. PMID:21282647 doi:https://dx.doi.org/10.1073/pnas.1006946108
↑Zhang C, Milunsky JM, Newton S, Ko J, Zhao G, Maher TA, Tager-Flusberg H, Bolliger MF, Carter AS, Boucard AA, Powell CM, Sudhof TC. A neuroligin-4 missense mutation associated with autism impairs neuroligin-4 folding and endoplasmic reticulum export. J Neurosci. 2009 Sep 2;29(35):10843-54. doi: 10.1523/JNEUROSCI.1248-09.2009. PMID:19726642 doi:https://dx.doi.org/10.1523/JNEUROSCI.1248-09.2009
↑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
