α-Synuclein mutations cluster around a putative protein loop

Neurosci Lett. 2013 Jun 24:546:67-70. doi: 10.1016/j.neulet.2013.04.058. Epub 2013 May 10.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Humans
  • Molecular Sequence Data
  • Multigene Family / genetics*
  • Point Mutation / genetics*
  • Protein Conformation
  • alpha-Synuclein / chemistry
  • alpha-Synuclein / genetics*
  • alpha-Synuclein / ultrastructure*

Substances

  • alpha-Synuclein