Structural and dynamic views of GM1 ganglioside

被引:20
|
作者
Yagi-Utsumi, Maho [1 ,2 ,3 ]
Kato, Koichi [1 ,2 ,3 ,4 ]
机构
[1] Natl Inst Nat Sci, Inst Mol Sci, Okazaki, Aichi 4448787, Japan
[2] Natl Inst Nat Sci, Okazaki Inst Integrat Biosci, Okazaki, Aichi 4448787, Japan
[3] Nagoya City Univ, Grad Sch Pharmaceut Sci, Mizuho Ku, Nagoya, Aichi 4678603, Japan
[4] Ochanomizu Univ, Glycosci Inst, Bunkyo Ku, Tokyo 1128610, Japan
关键词
Ganglioside GM1; Nuclearmagnetic resonance spectroscopy; Molecular dynamics simulation; Amyloid beta; alpha-synuclein; Bicelle; OLIGOSACCHARIDE CHAIN; PHOSPHOLIPID-BINDING; LIPID RAFTS; NMR; MEMBRANE; GLYCOSPHINGOLIPIDS; SURFACE; CONFORMATION; SPECTROSCOPY; ENSEMBLE;
D O I
10.1007/s10719-015-9587-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The ganglioside GM1 mediates various physiological and pathological processes mainly through the formation of GM1 clusters on cell surfaces. Therefore, detailed characterization of conformational properties of the glycan moiety of GM1 and the structures and interactions of this glycosphingolipid in membrane environments is necessary for better understanding of the clustering-coupled functional promotion. Nuclear magnetic resonance (NMR) spectroscopy has provided conformational information of GM1 in solution as well as in membrane-like environments. Recently, sophisticated paramagnetism-assisted NMR approaches combined with molecular dynamics simulations have enabled the quantitative exploration of conformational spaces of a series of gangliosides, including GM1, taking into account their minor conformations. NMR techniques have also been successfully applied to investigations of the dynamic interactions of GM1 clusters with amyloidogenic proteins such as amyloid beta and alpha-synuclein associated with neurodegenerative disorders. Further integration of experimental and computational approaches will open up new possibilities to provide structural views of the more complicated heterogeneous systems exemplified by microdomains involving GM1.
引用
收藏
页码:105 / 112
页数:8
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