title: Exploring the structural details of Cu(I) binding to α-synuclein by NMR spectroscopy.
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.
authors.affiliation: Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Universidad Nacional de Rosario, S2002LRK Rosario, Argentina.
authors.forename: Andres
authors.initials: A
authors.lastname: Binolfi
authors.forename: Ariel A
authors.initials: AA
authors.lastname: Valiente-Gabioud
authors.forename: Rosario
authors.initials: R
authors.lastname: Duran
authors.forename: Markus
authors.initials: M
authors.lastname: Zweckstetter
authors.forename: Christian
authors.initials: C
authors.lastname: Griesinger
authors.forename: Claudio O
authors.initials: CO
authors.lastname: Fernandez
mesh_terms: D003300:Copper / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D051844:alpha-Synuclein / Q000737:chemistry*
chemical_list: D051844:alpha-Synuclein; D003300:Copper