ArticleFEBS open bio2016
The 2.2-Angstrom resolution crystal structure of the carboxy-terminal region of ataxin-3.
Article in FEBS open bio, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Evolutionary model of repeat insertions in Ataxin-3 traces the origin of the polyglutamine stretch to an ancestral ubiquitin binding module.Protein science : a publication of the Protein Society · 2024Article
- ATXN3: a multifunctional protein involved in the polyglutamine disease spinocerebellar ataxia type 3.Expert reviews in molecular medicine · 2024Review
- Between Interactions and Aggregates: The PolyQ Balance.Genome biology and evolution · 2021Article
- Association with proteasome determines pathogenic threshold of polyglutamine expansion diseases.Biochemical and biophysical research communications · 2021Article
- Disentangling the complexity of low complexity proteins.Briefings in bioinformatics · 2020Review
- Machado-Joseph Deubiquitinases: From Cellular Functions to Potential Therapy Targets.Frontiers in pharmacology · 2020Review
- The Structural Properties in Solution of the Intrinsically Mixed Folded Protein Ataxin-3.Biophysical journal · 2018Article
- Identification of a novel site of interaction between ataxin-3 and the amyloid aggregation inhibitor polyglutamine binding peptide 1.European journal of mass spectrometry (Chichester, England) · 2018Article
- Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
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.
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