title: 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.
authors.affiliation: Reta Lila Weston Research Laboratories, Department of Molecular Neuroscience, UCL Institute of Neurology, London WC1N 3BG, UK. eleannakara@gmail.com
authors.forename: Eleanna
authors.initials: E
authors.lastname: Kara
authors.forename: Patrick A
authors.initials: PA
authors.lastname: Lewis
authors.forename: Helen
authors.initials: H
authors.lastname: Ling
authors.forename: Christos
authors.initials: C
authors.lastname: Proukakis
authors.forename: Henry
authors.initials: H
authors.lastname: Houlden
authors.forename: John
authors.initials: J
authors.lastname: Hardy
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D008969:Molecular Sequence Data; D005810:Multigene Family / Q000235:genetics*; D017354:Point Mutation / Q000235:genetics*; D011487:Protein Conformation; D051844:alpha-Synuclein / Q000737:chemistry / Q000235:genetics* / Q000648:ultrastructure*
chemical_list: D051844:alpha-Synuclein