Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis of myelin-associated glycoprotein adhesion and signalling.
Journal, issue, pages	Nat Commun, Vol. 7, Page 13584, Year 2016
Publish date	Dec 6, 2016
Authors	Matti F Pronker / Suzanne Lemstra / Joost Snijder / Albert J R Heck / Dominique M E Thies-Weesie / R Jeroen Pasterkamp / Bert J C Janssen /
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 ...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.
External links	Nat Commun / PubMed:27922006 / PubMed Central
Methods	SAS (X-ray synchrotron) / X-ray diffraction
Resolution	2.12 - 4.3 Å
Structure data	SASDB26: Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) I473E mutant Method: SAXS/SANS SASDB36: Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) N406Q mutant Method: SAXS/SANS SASDB46: Glycosylated Myelin-associated glycoprotein immunoglobulin domains 1-3 Method: SAXS/SANS SASDB55: Glycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5) Method: SAXS/SANS SASDB56: Deglycosylated myelin-associated glycoprotein full extracellular domain (Ig 1-5) I473E mutant Method: SAXS/SANS SASDB66: Deglycosylated myelin-associated glycoprotein full extracellular domain (Ig 1-5) N406Q mutant Method: SAXS/SANS SASDB76: Deglycosylated myelin-associated glycoprotein (immunoglobulin domains 1-3) Method: SAXS/SANS SASDBF6: Deglycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5) Method: SAXS/SANS PDB-5lf5: Myelin-associated glycoprotein (MAG) deglycosylated full extracellular domain with co-purified ligand Method: X-RAY DIFFRACTION / Resolution: 3.8 Å PDB-5lfr: Crystal structure of glycosylated Myelin-associated glycoprotein (MAG) Ig1-3 Method: X-RAY DIFFRACTION / Resolution: 2.12 Å PDB-5lfu: Myelin-associated glycoprotein (MAG) glycosylated and lysine-methylated full extracellular domain Method: X-RAY DIFFRACTION / Resolution: 4.3 Å PDB-5lfv: Crystal structure of glycosylated Myelin-associated glycoprotein (MAG) Ig1-3 with soaked trisaccharide ligand Method: X-RAY DIFFRACTION / Resolution: 2.3 Å
Chemicals	ChemComp-MAN: alpha-D-mannopyranose ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-GOL: GLYCEROL ChemComp-SO4: SULFATE ION ChemComp-HOH: WATER
Source	mus musculus (house mouse)
Keywords	CELL ADHESION / Myelin / Signaling / cell adhesion molecule