Parkinson's disease (PD) is a progressive disorder of the central nervous system affecting more than 1 million people in the United States. PD is caused by the degeneration of dopamine-producing cells in the brain. Since dopamine itself cannot pass through the blood-brain barrier, the standard treatment for PD is administration of levodopa, which can reach the brain where it is converted to dopamine. A problem with this compound is that it can also be converted to dopamine in the bloodstream, leading to unwanted side effects. One way to mitigate this problem is to administer inhibitors of DOPA decarboxylase, the enzyme that converts levodopa to dopamine in the blood.
In the November issue of Nature Structural Biology (Vol. 8, No. 11, pages 963-967), Peter Burhard of the M. E. Muller Institute for Structural Biology at the University of Basel, Switzerland and his collaborators describe the structure of DOPA decarboxylase with carbiDOPA, an inhibitor used in Parkinson's disease treatment. The structure reveals how this drug binds its target enzyme and suggests ways to design inhibitors that bind more tightly and more specifically, possibly leading to better treatments for Parkinson's and other neurological diseases.
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