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Publication Detail
α-Synuclein mutations cluster around a putative protein loop.
Abstract
With the recent identification of two new pathogenic mutations in α-synuclein, we map the five known pathogenic mutations onto the best available models of the protein structure. We show that four of the five mutations map to a potential fold in the protein with the exception being the A30P mutation in which the substitution would be expected to have a profound effect on protein structure. We discuss this localisation in terms of the proposed mechanisms for mutation pathogenicity.
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Neurodegenerative Diseases
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Department of Neuromuscular Diseases
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Clinical and Movement Neurosciences
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Clinical and Movement Neurosciences
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