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| | <StructureSection load='5lfu' size='340' side='right'caption='[[5lfu]], [[Resolution|resolution]] 4.30Å' scene=''> | | <StructureSection load='5lfu' size='340' side='right'caption='[[5lfu]], [[Resolution|resolution]] 4.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lfu]] is a 1 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=5LFU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LFU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lfu]] is a 1 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=5LFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LFU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</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]] 4.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mag ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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://proteopedia.org/fgij/fg.htm?mol=5lfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfu OCA], [http://pdbe.org/5lfu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lfu RCSB], [http://www.ebi.ac.uk/pdbsum/5lfu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfu 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=5lfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfu OCA], [https://pdbe.org/5lfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lfu RCSB], [https://www.ebi.ac.uk/pdbsum/5lfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MAG_MOUSE MAG_MOUSE]] Adhesion molecule in postnatal neural development that mediates sialic-acid dependent cell-cell interactions between neuronal and myelinating cells. Preferentially binds to alpha-2,3-linked sialic acid. Isoform L-MAG is critical for the formation of myelin in the CNS, whereas isoform S-MAG is sufficient to maintain the integrity of myelin in PNS.<ref>PMID:10625334</ref> | + | [https://www.uniprot.org/uniprot/MAG_MOUSE MAG_MOUSE] Adhesion molecule in postnatal neural development that mediates sialic-acid dependent cell-cell interactions between neuronal and myelinating cells. Preferentially binds to alpha-2,3-linked sialic acid. Isoform L-MAG is critical for the formation of myelin in the CNS, whereas isoform S-MAG is sufficient to maintain the integrity of myelin in PNS.<ref>PMID:10625334</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Janssen, B J.C]] | + | [[Category: Janssen BJC]] |
| - | [[Category: Pronker, M F]] | + | [[Category: Pronker MF]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Myelin]]
| + | |
| - | [[Category: Signaling]]
| + | |
| Structural highlights
Function
MAG_MOUSE Adhesion molecule in postnatal neural development that mediates sialic-acid dependent cell-cell interactions between neuronal and myelinating cells. Preferentially binds to alpha-2,3-linked sialic acid. Isoform L-MAG is critical for the formation of myelin in the CNS, whereas isoform S-MAG is sufficient to maintain the integrity of myelin in PNS.[1]
Publication Abstract from PubMed
Myelin-associated glycoprotein (MAG) is a myelin-expressed cell-adhesion and bi-directional signalling molecule. MAG maintains the myelin-axon spacing by interacting with specific neuronal glycolipids (gangliosides), inhibits axon regeneration and controls myelin formation. The mechanisms underlying MAG adhesion and signalling are unresolved. We present crystal structures of the MAG full ectodomain, which reveal an extended conformation of five Ig domains and a homodimeric arrangement involving membrane-proximal domains Ig4 and Ig5. MAG-oligosaccharide complex structures and biophysical assays show how MAG engages axonal gangliosides at domain Ig1. Two post-translational modifications were identified-N-linked glycosylation at the dimerization interface and tryptophan C-mannosylation proximal to the ganglioside binding site-that appear to have regulatory functions. Structure-guided mutations and neurite outgrowth assays demonstrate MAG dimerization and carbohydrate recognition are essential for its regeneration-inhibiting properties. The combination of trans ganglioside binding and cis homodimerization explains how MAG maintains the myelin-axon spacing and provides a mechanism for MAG-mediated bi-directional signalling.
Structural basis of myelin-associated glycoprotein adhesion and signalling.,Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ Nat Commun. 2016 Dec 6;7:13584. doi: 10.1038/ncomms13584. PMID:27922006[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schachner M, Bartsch U. Multiple functions of the myelin-associated glycoprotein MAG (siglec-4a) in formation and maintenance of myelin. Glia. 2000 Jan 15;29(2):154-65. PMID:10625334
- ↑ Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ. Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun. 2016 Dec 6;7:13584. doi: 10.1038/ncomms13584. PMID:27922006 doi:http://dx.doi.org/10.1038/ncomms13584
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