Abstract
Huntington's disease (HD) arises from an expanded polyglutamine (polyQ) in the N-terminus of the huntingtin (htt) protein. Neuronal degeneration and inclusions containing N-terminal fragments of mutant htt are present in the cortex and striatum of HD brain. Recently, a model of polyQ aggregate structure has been proposed on the basis of studies with synthetic polyQ peptides and includes an alternating beta-strand/beta-turn structure with seven glutamine residues per beta-strand. We tested this model in the context of the htt exon-1 N-terminal fragment in both mammalian cell culture and cultured primary cortical neurons. We found our data support this model in the htt protein and provide a better understanding of the structural basis of polyQ aggregation in toxicity in HD.
Original language | English (US) |
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Pages (from-to) | 765-774 |
Number of pages | 10 |
Journal | Human molecular genetics |
Volume | 14 |
Issue number | 6 |
DOIs | |
State | Published - Mar 15 2005 |
ASJC Scopus subject areas
- Molecular Biology
- Genetics
- Genetics(clinical)