Researchers have discovered a number of proteins that increase the misfolding of ataxin-1, a process known to contribute to the disease and Huntington’s disease several other neurological diseases.
ataxin-1 is a protein in the brain is vulnerable to misfolding due to an inherited genetic defect. This is caused by the repetition of the amino acid glutamine in the amino acid chain of the protein. High levels of glutamine – about more than 40 repetitions – cause toxic protein
A team from the Max Delbrück Center for Molecular Medicine (MDC) Berlin-Buch, Germany and the University Paris Diderot in France have identified. 21 proteins that bind to ataxin-1, 12 of which are known to improve processes misfolding by increasing toxicity.
The researchers also noted a common feature in the structure of 12 proteins that increase toxicity, known as coiled-coil domain. This resembles a double spiral twisted and promotes aggregation.
Now this structure is believed it could present an opportunity for targeted therapy “suppress toxic processes.”
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Posted in: Huntington's Disease