Pathogenic and Non-pathogenic Polyglutamine Tracts Have Similar Structural Properties: Towards a Length-dependent Toxicity Gradient

• Published in: Journal of molecular biology Vol. 371; no. 1; pp. 235 - 244
• Main Authors: Klein, Fabrice A.C., Pastore, Annalisa, Masino, Laura, Zeder-Lutz, Gabrielle, Nierengarten, Hélène, Oulad-Abdelghani, Mustapha, Altschuh, Danièle, Mandel, Jean-Louis, Trottier, Yvon
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 03.08.2007; Elsevier
• Subjects: Amino Acid Sequence; Biochemistry, Molecular Biology; expansion; Humans; Life Sciences; Molecular biology; Neurodegenerative Diseases; Neurodegenerative Diseases - metabolism; Nuclear Magnetic Resonance, Biomolecular; Peptides; Peptides - chemistry; Peptides - genetics; Peptides - metabolism; polyglutamine; Proteins; Proteins - genetics; Proteins - toxicity; structure; threshold; toxicity; toxicity; RU; Fab; GST; threshold; polyglutamine; structure; expansion; ESI-TOF; SPR; polyQ; HSQC; Qn

Abnormally expanded polyglutamine (polyQ) tracts provide a gain of toxic functions to nine otherwise unrelated human proteins and induce progressive neurodegenerative diseases. Over the past ten years, it was suggested that only polyQ tracts longer than a specific threshold adopt a particular struct...