The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3

Vladimir A. Zhemkov, Anna A. Kulminskaya, Ilya B. Bezprozvanny, Meewhi Kim

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


An expansion of polyglutamine (polyQ) sequence in ataxin-3 protein causes spinocerebellar ataxia type 3, an inherited neurodegenerative disorder. The crystal structure of the polyQ-containing carboxy-terminal fragment of human ataxin-3 was solved at 2.2-Å resolution. The Atxn3 carboxy-terminal fragment including 14 glutamine residues adopts both random coil and α-helical conformations in the crystal structure. The polyQ sequence in α-helical structure is stabilized by intrahelical hydrogen bonds mediated by glutamine side chains. The intrahelical hydrogen-bond interactions between glutamine side chains along the axis of the polyQ α-helix stabilize the secondary structure. Analysis of this structure furthers our understanding of the polyQ-structural characteristics that likely underlie the pathogenesis of polyQ-expansion disorders.

Original languageEnglish (US)
Pages (from-to)168-178
Number of pages11
JournalFEBS Open Bio
Issue number3
StatePublished - Feb 1 2016


  • Ataxia
  • Ataxins
  • Huntington's disease
  • Polyglutamine
  • Triplet repeat disorder

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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