Possible tetrameric structure of a-synuclein.IMAGE COURTESY OF HARVARD MEDICAL SCHOOL.
New findings, published this week in Nature, challenge the long-standing view that a-synuclein, a protein involved in Parkinson's disease, is a single, unfolded protein. Instead, the protein appears helical in shape, and is composed of four synuclein components. The results suggest an extra step in the process of protein clumping, in which the tetramer first falls apart into its individual protein parts before congealing into the fibrils seen in Parkinson's disease.
The results “really fit with what I was already thinking,” said Julia George, a professor at the University of Illinois, and who was not a researcher on this study. Other groups had previously found evidence that a-synuclein could take shape as a helical tetramer, but the new study is the first to suggest that ...
