Copper(II) binding to alpha-synuclein, the Parkinson's protein.
Variations in tryptophan fluorescence intensities confirm that copper(II) interacts with alpha-synuclein, a protein implicated in Parkinson's disease. Trp4 fluorescence decay kinetics measured for the F4W protein show that Cu(II) binds tightly (Kd 100 nM) near the N-terminus at pH 7. Work on a F4W/H50S mutant indicates that a histidine imidazole is not a ligand in this high-affinity site.
Lee
Jennifer C
JC
Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-8013, USA. leej4@mail.nih.gov
Gray
Harry B
HB
Winkler
Jay R
JR
D000595:Amino Acid Sequence; D001665:Binding Sites; D002413:Cations, Divalent / Q000737:chemistry; D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D005453:Fluorescence; D006801:Humans; D007381:Intermediate Filament Proteins / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D017354:Point Mutation; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000737:chemistry / Q000378:metabolism
D002413:Cations, Divalent; D007381:Intermediate Filament Proteins; C430456:desmuslin; D003300:Copper; D014364:Tryptophan