Journal
ACS CHEMICAL NEUROSCIENCE
Volume 10, Issue 3, Pages 1135-1136Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acschemneuro.9b00090
Keywords
Alpha-synuclein; cryo-EM; Greek key; protofilament; steric zipper; Parkinson's disease
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Recent expeditious advances in the determination of the 3-D structure of fibrils of alpha-synuclein, the intrinsically disordered protein associated with the neurodegenerative Parkinson's disease (PD), have identified amino acid contacts that form the fibril's inter-protofilament interface. The residues that constitute this steric zipper interface determine the morphology of the fibrils as well as toxicity of the oligomeric building units or kernels which lead to the formation of the protofilaments. The zipper interface houses key amino acid residues involved in familial PD that can be targeted by drug design.
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