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Published on: May 30, 2021
Exploring the structural details of Cu(I) binding to α-synuclein by NMR spectroscopy
Andres Binolfi1, Ariel A Valiente-Gabioud, Rosario Duran
1Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Universidad Nacional de Rosario, S2002LRK Rosario, Argentina.
Abstract:
The aggregation of α-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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