Protein discovery could have implication for Huntington's disease

Researchers have discovered a series of proteins that increase the misfolding of ataxin-1, a process known to contribute to Huntington's disease and various other neurological diseases.

Ataxin-1 is a protein in the brain that is vulnerable to misfolding because of an inherited gene defect. This is caused by the repetition of amino acid glutamine in the amino acid chain of the protein. High levels of glutamine - approximately over 40 repeats - make the protein toxic.

A team at the Max Delbrück Center for Molecular Medicine (MDC) Berlin-Buch, Germany and the Université Paris Diderot in France has now identified 21 proteins that bind to ataxin-1, 12 of which are known to enhance misfolding processes by increasing toxicity.

Researchers also observed a common feature in the structure of the 12 proteins that increase toxicity, known as coiled-coil-domain. This resembles a double twisted spiral and promotes aggregation.

It is now believed this structure could present an opportunity for targeted therapy to "suppress toxic processes".

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