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5lfr

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Crystal structure of glycosylated Myelin-associated glycoprotein (MAG) Ig1-3

Structural highlights

5lfr is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.12Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5lfr"

Categories: Large Structures | Mus musculus | Janssen BJC | Pronker MF

@@ Line 1: / Line 1: @@
 ==Crystal structure of glycosylated Myelin-associated glycoprotein (MAG) Ig1-3==
-<StructureSection load='5lfr' size='340' side='right' caption='[[5lfr]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
+<StructureSection load='5lfr' size='340' side='right'caption='[[5lfr]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5lfr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LFR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5lfr]] 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=5LFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LFR FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.12&#8491;</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=5lfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfr OCA], [http://pdbe.org/5lfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lfr RCSB], [http://www.ebi.ac.uk/pdbsum/5lfr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfr ProSAT]</span></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5lfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfr OCA], [https://pdbe.org/5lfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lfr RCSB], [https://www.ebi.ac.uk/pdbsum/5lfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfr ProSAT]</span></td></tr>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Janssen, B J.C]]
+[[Category: Large Structures]]
-[[Category: Pronker, M F]]
+[[Category: Mus musculus]]
-[[Category: Cell adhesion]]
+[[Category: Janssen BJC]]
-[[Category: Cell adhesion molecule]]
+[[Category: Pronker MF]]
-[[Category: Myelin]]

5lfr

From Proteopedia

Current revision

Crystal structure of glycosylated Myelin-associated glycoprotein (MAG) Ig1-3

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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