Glutamine repeats: structural hypotheses and neurodegeneration. (August 2002)

• Record Type: Journal Article
• Authors: Masino, L.; Pastore, A.
• Is Part Of: Biochemical Society transactions. Volume 30:Number 4(2002)
• Page Start: 548
• Page End: 551
• Publication Date: 2002-08
• Subjects: aggregation -- neurodegenerative disease -- polyglutamine -- structure; CI2, chymotrypsin inhibitor 2 -- GST, glutathione S-transferase -- SCA, spinocerebellar ataxia; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0300548
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : A growing number of neurodegenerative diseases are caused by expansion of CAG trinucleotide repeats coding for polyglutamine. The presence of intranuclear inclusions in the affected neuronal cells has suggested a mechanism for pathogenesis based on protein misfolding and aggregation. Detailed understanding of these phenomena is therefore crucial in order to rationalize different phases of the diseases. In the past decade, a few studies have focused on the structural properties of polyglutamine and on the molecular bases of the aggregation process. Most of these studies have been performed on polyglutamine peptides and protein models. Only one report is currently available on the characterization of a full-length polyglutamine protein. The structural hypotheses resulting from these studies are reviewed here.