Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy
Journal of the American Chemical Society2010Vol. 133(2), pp. 194–196
Citations Over TimeTop 13% of 2010 papers
Andrés Binolfi, Ariel A. Valiente‐Gabioud, Rosario Durán, Markus Zweckstetter, Christian Griesinger, Claudio O. Fernández
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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