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5LFR

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

Summary for 5LFR
Entry DOI10.2210/pdb5lfr/pdb
DescriptorMyelin-associated glycoprotein, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
Functional Keywordsmyelin, cell adhesion molecule, cell adhesion
Biological sourceMus musculus (House Mouse)
Cellular locationCell membrane ; Single-pass type I membrane protein : P20917
Total number of polymer chains2
Total formula weight74099.27
Authors
Pronker, M.F.,Janssen, B.J.C. (deposition date: 2016-07-04, release date: 2016-12-14, Last modification date: 2024-10-23)
Primary citationPronker, M.F.,Lemstra, S.,Snijder, J.,Heck, A.J.,Thies-Weesie, D.M.,Pasterkamp, R.J.,Janssen, B.J.
Structural basis of myelin-associated glycoprotein adhesion and signalling.
Nat Commun, 7:13584-13584, 2016
Cited by
PubMed Abstract: 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.
PubMed: 27922006
DOI: 10.1038/ncomms13584
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.12 Å)
Structure validation

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