Huntingtin's spherical solenoid structure enables polyglutamine tract-dependent modulation of its structure and function.

This work mapped out phosphorylation sites across huntingtin, and showed a trend of all sites being hypo-phosphorylated due to polyglutamine expansion, even near the carboxyl-terminus. 4) The authors claim in the Abstract that they provide the first glimpse into the structural properties of huntingtin and an elegant solution to the apparent conundrum of how the extreme amino-terminal polyglutamine tract confers a novel property on huntingtin, causing the disease.

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