Ultra-high field NMR studies of antibody binding and site-specific phosphorylation of alpha-synuclein.
Although biological importance of intrinsically disordered proteins is becoming recognized, NMR analyses of this class of proteins remain as tasks with more challenge because of poor chemical shift dispersion. It is expected that ultra-high field NMR spectroscopy offers improved resolution to cope with this difficulty. Here, we report an ultra-high field NMR study of alpha-synuclein, an intrinsically disordered protein identified as the major component of the Lewy bodies. Based on NMR spectral data collected at a 920 MHz proton frequency, we performed epitope mapping of an anti-alpha-synuclein monoclonal antibody, and furthermore, characterized conformational effects of phosphorylation at Ser129 of alpha-synuclein.
Sasakawa
Hiroaki
H
Department of Structural Biology and Biomolecular Engineering, Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan.
Sakata
Eri
E
Yamaguchi
Yoshiki
Y
Masuda
Masami
M
Mori
Tetsuya
T
Kurimoto
Eiji
E
Iguchi
Takeshi
T
Hisanaga
Shin-ichi
S
Iwatsubo
Takeshi
T
Hasegawa
Masato
M
Kato
Koichi
K
D000911:Antibodies, Monoclonal / Q000276:immunology / Q000378:metabolism*; D001665:Binding Sites; D018604:Epitope Mapping; D000939:Epitopes / Q000276:immunology / Q000378:metabolism; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009154:Mutation; D010766:Phosphorylation; D012694:Serine / Q000235:genetics / Q000378:metabolism; D051844:alpha-Synuclein / Q000235:genetics / Q000276:immunology / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D000939:Epitopes; D051844:alpha-Synuclein; D012694:Serine