Investigating the familial Parkinson's disease's mutations in DJ-1 and their affect on the 20S proteasome

摘要

The altered conformations of the different mutations, like the lack of dimerization or unfolded state suggest that the protein has impaired activity and possibly impaired binding and inhibition of the 20S proteasome. Their interaction with the 20S proteasome should be tested in order to see if they have a different effect on the binding or the inhibition of the 20S proteasome, than the wild type form.