This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5lfu

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Myelin-associated glycoprotein (MAG) glycosylated and lysine-methylated full extracellular domain

Structural highlights

5lfu is a 1 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 4.3Å
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/5lfu"

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

@@ Line 3: / Line 3: @@
 <StructureSection load='5lfu' size='340' side='right'caption='[[5lfu]], [[Resolution|resolution]] 4.30&Aring;' scene=''>
 == 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]] 4.3&#8491;</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>
 == 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 24: / Line 24: @@
 </StructureSection>
 [[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]]

5lfu

From Proteopedia

Current revision

Myelin-associated glycoprotein (MAG) glycosylated and lysine-methylated full extracellular domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox