Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 133, Issue 2, Pages 194-196Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja107842f
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Funding
- ANPCyT [PME2003-2006]
- Fundacion Antorchas
- CONICET
- Max Planck Society
- Alexander von Humboldt Foundation
- DFG [ZW 71/2-2, 2-3]
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The aggregation of alpha-synuclein (AS) is selectively enhanced by copper in vitro, and the interaction is proposed to play a potential role in vivo. In this work, we report the structural, residue-specific characterization of Cu(I) binding to AS and demonstrate that the protein is able to bind Cu(I) with relatively high affinity in a coordination environment that involves the participation of Met1 and Met5 residues. This knowledge is a key to understanding the structural-aggregation basis of the copper-catalyzed oxidation of AS.
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