@ARTICLE{10.3389/fnmol.2016.00048, AUTHOR={Wang, Chuchu and Zhao, Chunyu and Li, Dan and Tian, Zhiqi and Lai, Ying and Diao, Jiajie and Liu, Cong}, TITLE={Versatile Structures of α-Synuclein}, JOURNAL={Frontiers in Molecular Neuroscience}, VOLUME={9}, YEAR={2016}, URL={https://www.frontiersin.org/articles/10.3389/fnmol.2016.00048}, DOI={10.3389/fnmol.2016.00048}, ISSN={1662-5099}, ABSTRACT={α-Synuclein (α-syn) is an intrinsically disordered protein abundantly distributed in presynaptic terminals. Aggregation of α-syn into Lewy bodies (LB) is a molecular hallmark of Parkinson’s disease (PD). α-Syn features an extreme conformational diversity, which adapts to different conditions and fulfills versatile functions. However, the molecular mechanism of α-syn transformation and the relation between different structural species and their functional and pathogenic roles in neuronal activities and PD remain unknown. In this mini-review, we summarize the recent discoveries of α-syn structures in the membrane-bound state, in cytosol, and in the amyloid state under physiological and pathological conditions. From the current knowledge on different structural species of α-syn, we intend to find a clue about its function and toxicity in normal neurons and under disease conditions, which could shed light on the PD pathogenesis.} }