Molecular structures provide roadmap for targeted Parkinson's disease therapeutics
Researchers at Weill Cornell Medicine have uncovered how a key Parkinson's protein called LRRK2 shifts between inactive and active forms, revealing the structural changes that enable certain mutations to push the protein into an overactive state. Mutations that cause LRRK2 to become abnormally active are among the most common genetic causes of Parkinson's disease. Even without these mutations,…
Scientists at Weill Cornell Medicine have discovered how the Parkinson's protein LRRK2 switches between inactive and active states. This finding could pave the way for new targeted treatments for Parkinson's disease. LRRK2 is a protein with seven domains, some of which help it attach to other proteins and structures inside cells, while two domains have different enzymatic activities.
Mutations that cause LRRK2 to become overactive are a major genetic cause of Parkinson's disease, and even without mutations, some people with the disease have elevated LRRK2 activity. By capturing LRRK2 in different structural states and analyzing the changes, researchers were able to understand how the protein toggles between active and inactive forms.
The study, published in Cell, points toward potential new drugs that can selectively control LRRK2 activity, offering hope for a more precise and less harmful approach to treating Parkinson's disease.
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