Binding Epitopes of Gangliosides to their Neuronal Receptor, Myelin-Associated Glycoprotein, from Saturation Transfer Difference NMR

MAGnificent analysis to remove ambiguity: The binding epitopes of tri‐ and tetrasaccharide ligands in their interactions with the myelin‐associated glycoprotein (MAG) have been studied by using saturation transfer difference NMR, in which the signal intensities can help to resolve overlapped HSQC si...

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Published inChembiochem : a European journal of chemical biology Vol. 9; no. 18; pp. 2946 - 2949
Main Authors Shin, So-Young, Gäthje, Heiko, Schwardt, Oliver, Gao, Gan-Pan, Ernst, Beat, Kelm, Soerge, Meyer, Bernd
Format Journal Article
LanguageEnglish
Published Weinheim Wiley-VCH Verlag 15.12.2008
WILEY‐VCH Verlag
Subjects
axonal regeneration
Binding Sites
Carbohydrate Conformation
carbohydrates
epitopes
Epitopes - metabolism
Gangliosides - chemistry
Gangliosides - pharmacology
Myelin-Associated Glycoprotein - antagonists & inhibitors
Myelin-Associated Glycoprotein - chemistry
Myelin-Associated Glycoprotein - metabolism
myelin‐associated glycoprotein
Nuclear Magnetic Resonance, Biomolecular
saturation transfer difference NMR
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Summary:MAGnificent analysis to remove ambiguity: The binding epitopes of tri‐ and tetrasaccharide ligands in their interactions with the myelin‐associated glycoprotein (MAG) have been studied by using saturation transfer difference NMR, in which the signal intensities can help to resolve overlapped HSQC signals. In the figure, the signals of the protons with the closest proximity to the protein are shown in red (30–60 %) or blue (61–100 %).
Bibliography:http://dx.doi.org/10.1002/cbic.200800485
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ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200800485