Neuroligin: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Jaime Prilusky, David Canner, Michal Harel, Pascale Marchot, Joel L. Sussman

@@ Line 1: / Line 1: @@
-[[Image:3be8a.png|left|200px|thumb|Crystal Structure of human Neuroligin [[3be8]]]]
+<StructureSection load='' size='350' side='right' scene='42/422448/Cv/2' caption='Dimer of two mouse neuroligin-1 cholinesterase-like domains (magenta and cyan) in complex with two neurexin-beta1 LNS6 domains (salmon and yellow) and Ca+2 ions (green) [[3b3q]]'>
-{{STRUCTURE_3b3q|  PDB=3b3q  | SIZE=400| SCENE= |right|CAPTION=Mouse neuroligin 1 LNS domain dimer (grey and green) complex with neurexin cholinesterase-like domain (pink and cyan) and Ca+2 ions [[3b3q]] }}
+== Function ==
+[[Neuroligin|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<ref>PMID:18093521</ref>.
+See [[Neurodevelopmental Disorders]]<br />
+[[Neuroligin-Neurexin Interaction]]
+*'''NLGN-1''' regulates spines and synaptic plasticity<ref>PMID:26880202</ref>. <br />
+*'''NLGN-2''' is localized to inhibitory synapses<ref>PMID:15540461</ref>. <br />
+*'''NLGN-3''' is a synapse organizer which shapes normal function and autism disorder<ref>PMID:17897391</ref>. <br />
+*'''NLGN-4''' is localized to glyceric  post-synapses and regulates retina inhibition<ref>PMID:21282647</ref>. <br />
+== Disease ==
+Mutations in NLGN 4 are associated with autism and mental retardation<ref>PMID:19726642</ref>.
+== Structural insights ==
+The <scene name='42/422448/Cv/5'>NLGN-NRXN complex involves the octahedrally coordinated Ca+2 ion</scene><ref>PMID:18084303</ref>. Water molecules are shown as red spheres.
+</StructureSection>
-[[Neuroligin|Neuroligins]] (NLGN) are a family of postsynaptic proteins which bind to the presynaptic [[Neurexin]] (NRXN) to form a complex which attaches neurons.  The NLGN family contains 4 members which are numbered 1 to 4.
-For Structural Analysis of Neuroligin, See: [[Neuroligin-Neurexin Interaction]]
-{{TOC limit|limit=2}}
 == 3D Structures of Neuroligin ==
+{{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+{{#tree:id=OrganizedByTopic|openlevels=0|
-=== NLGN ===
+* Neuroligin
+**[[5ojk]] -  hNLGN-1 cholinesterase domain - human<br />
+**[[3bix]] -  rNLGN-1 cholinesterase domain - rat<br />
+**[[8gs4]] -  hNLGN-2 – Cryo EM<br />
+**[[3bl8]] -  mNLGN-2 cholinesterase domain – mouse<br />
+**[[7cee]] - mNLGN-3 cholinesterase domain<br />
+**[[3be8]] -  hNLGN-4 cholinesterase domain – human<br />
-[[3bl8]] -  mNLGN-2 cholinesterase domain – mouse<br />
+* Neuroligin+neurexin
-[[3be8]] -  hNLGN-4 cholinesterase domain – human<br />
-[[3bix]] -  rNLGN-1 cholinesterase domain - rat<br />
+**[[2xb6]], [[2wqz]] – hNLGN-4 cholinesterase domain+NRXN-1β LNS domain <br />
+**[[3b3q]] -  mNLGN-4 cholinesterase domain+NRXN-1β LNS domain<br />
+**[[3biw]] -  rNLGN-1 cholinesterase domain+NRXN-1β LNS domain<br />
+**[[3vkf]] - rNLGN-1 cholinesterase domain + bNRXN-1β LNS domain
-=== NLGN+NRXN ===
+*NLGN other complexes
-[[2xb6]], [[2wqz]] – hNLGN-4 cholinesterase domain+NRXN-1β LNS domain <br />
+**[[5oj6]] -  rNLGN-1 cholinesterase domain + MDGA1<br />
-[[3b3q]] -  mNLGN-4 cholinesterase domain+NRXN-1β LNS domain<br />
+**[[5v5v]] -  rNLGN-2 cholinesterase domain + MDGA1<br />
-[[3biw]] -  rNLGN-1 cholinesterase domain+NRXN-1β LNS domain<br />
+**[[5xeq]] -  rNLGN-2 cholinesterase domain (mutant) + MDGA1<br />
+**[[7ceg]] -  mNLGN-3 cholinesterase domain + PTP d<br />
+}}
+== References ==
+<references/>
 [[Category:Topic Page]]