Structural switching of Cu,Zn-superoxide dismutases at loop VI: insights from the crystal structure of 2-mercaptoethanol-modified enzyme

Structural switching of Cu,Zn-superoxide dismutases at loop VI: insights from the crystal structure of 2-mercaptoethanol-modified enzyme

Cu,Zn SOD1 (superoxide dismutase 1) is implicated in FALS (familial amyotrophic lateral sclerosis) through the accumulation of misfolded proteins that are toxic to neuronal cells. Loop VI (residues 102–115) of the protein is at the dimer interface and could play a critical role in stabili...

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Bibliographic Details
Main Authors: Kentaro Ihara, Noriko Fujiwara, Yoshiki Yamaguchi, Hidetaka Torigoe, Soichi Wakatsuki, Naoyuki Taniguchi, Keiichiro Suzuki
Format: Article
Language:English
Published: Portland Press, Biochemical Society 2012-09-01
Series:Bioscience Reports
Subjects:
superoxide dismutase 1 (SOD1)
crystal structure
amyotrophic lateral sclerosis (ALS)
asymmetric configuration
Online Access:http://www.bioscirep.org/bsr/032/0539/bsr0320539.htm

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http://www.bioscirep.org/bsr/032/0539/bsr0320539.htm

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