Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy.
 

Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy.

Exploring the Structural Details of Cu(I) Binding to ?-Synuclein by NMR Spectroscopy.

J Am Chem Soc. 2010 Dec 15;

Authors: Binolfi A, Valiente-Gabioud AA, Duran R, Zweckstetter M, Griesinger C, Fernandez CO

The aggregation of ?-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.

PMID: 21158432 [PubMed - as supplied by publisher]



Source: PubMed