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| - | ==CRYSTAL STRUCTURE OF THE N-TERMINAL LEUCINE RICH REPEATS OF NETRIN-G LIGAND-3== | + | ==Crystal structure of the N-terminal leucine rich repeats of Netrin-G Ligand-3== |
| - | <StructureSection load='3zyn' size='340' side='right' caption='[[3zyn]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='3zyn' size='340' side='right'caption='[[3zyn]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zyn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZYN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zyn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZYN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 3.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zyo|3zyo]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=3zyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zyn OCA], [http://pdbe.org/3zyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zyn RCSB], [http://www.ebi.ac.uk/pdbsum/3zyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zyn ProSAT]</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=3zyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zyn OCA], [https://pdbe.org/3zyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zyn RCSB], [https://www.ebi.ac.uk/pdbsum/3zyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zyn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LRC4B_MOUSE LRC4B_MOUSE]] Synaptic adhesion protein. Regulates the formation of excitatory synapses. The trans-synaptic adhesion between LRRC4B and PTPRF regulates the formation of excitatory synapses in a bidirectional manner (By similarity). | + | [https://www.uniprot.org/uniprot/LRC4B_MOUSE LRC4B_MOUSE] Synaptic adhesion protein. Regulates the formation of excitatory synapses. The trans-synaptic adhesion between LRRC4B and PTPRF regulates the formation of excitatory synapses in a bidirectional manner (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Aricescu, A R]] | + | [[Category: Mus musculus]] |
| - | [[Category: Coles, C H]] | + | [[Category: Aricescu AR]] |
| - | [[Category: Harlos, K]] | + | [[Category: Coles CH]] |
| - | [[Category: Jones, E Y]] | + | [[Category: Harlos K]] |
| - | [[Category: Mcilhinney, R A.J]] | + | [[Category: Jones EY]] |
| - | [[Category: Perestenko, P V]] | + | [[Category: McIlhinney RAJ]] |
| - | [[Category: Seiradake, E]] | + | [[Category: Perestenko PV]] |
| - | [[Category: Cell adhesion]]
| + | [[Category: Seiradake E]] |
| - | [[Category: Synapse]]
| + | |
| Structural highlights
Function
LRC4B_MOUSE Synaptic adhesion protein. Regulates the formation of excitatory synapses. The trans-synaptic adhesion between LRRC4B and PTPRF regulates the formation of excitatory synapses in a bidirectional manner (By similarity).
Publication Abstract from PubMed
Brain wiring depends on cells making highly localized and selective connections through surface protein-protein interactions, including those between NetrinGs and NetrinG ligands (NGLs). The NetrinGs are members of the structurally uncharacterized netrin family. We present a comprehensive crystallographic analysis comprising NetrinG1-NGL1 and NetrinG2-NGL2 complexes, unliganded NetrinG2 and NGL3. Cognate NetrinG-NGL interactions depend on three specificity-conferring NetrinG loops, clasped tightly by matching NGL surfaces. We engineered these NGL surfaces to implant custom-made affinities for NetrinG1 and NetrinG2. In a cellular patterning assay, we demonstrate that NetrinG-binding selectivity can direct the sorting of a mixed population of NGLs into discrete cell surface subdomains. These results provide a molecular model for selectivity-based patterning in a neuronal recognition system, dysregulation of which is associated with severe neuropsychological disorders.
Structural basis for cell surface patterning through NetrinG-NGL interactions.,Seiradake E, Coles CH, Perestenko PV, Harlos K, McIlhinney RA, Aricescu AR, Jones EY EMBO J. 2011 Sep 23. doi: 10.1038/emboj.2011.346. PMID:21946559[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Seiradake E, Coles CH, Perestenko PV, Harlos K, McIlhinney RA, Aricescu AR, Jones EY. Structural basis for cell surface patterning through NetrinG-NGL interactions. EMBO J. 2011 Sep 23. doi: 10.1038/emboj.2011.346. PMID:21946559 doi:10.1038/emboj.2011.346
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