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A soluble α-synuclein construct forms a dynamic tetramer
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DOI：10.1073/pnas.1113260108.png)
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Abstract
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A heterologously expressed form of the human Parkinson disease-associated protein alpha-synuclein with a 10-residue N-terminal extension is shown to form a stable tetramer in the absence of lipid bilayers or micelles. Sequential NMR assignments, intramonomer nuclear Overhauser effects, and circular dichroism spectra are consistent with transient formation of alpha-helices in the first 100 N-terminal residues of the 140-residue alpha-synuclein sequence. Total phosphorus analysis indicates that phospholipids are not associated with the tetramer as isolated, and chemical cross-linking experiments confirm that the tetramer is the highest-order oligomer present at NMR sample concentrations. Image reconstruction from electron micrographs indicates that a symmetric oligomer is present, with three- or fourfold symmetry. Thermal unfolding experiments indicate that a hydrophobic core is present in the tetramer. A dynamic model for the tetramer structure is proposed, based on expected close association of the amphipathic central helices observed in the previously described micelle-associated hairpin structure of alpha-synuclein.
Keywords:
dynamic structure
helical
Parkinson's disease
NMR
heteronuclear single-quantum coherence
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