期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 119, 期 31, 页码 10005-10015出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.5b03760
关键词
-
资金
- [303741]
alpha-Synuclein (AS) fibrils are the major hallmarks of Parkinson's disease (PD). It is known that the central domain of the 140-residue AS protein, known as the non-amyloid-beta component (NAC), plays a crucial role in aggregation. The secondary structure of AS fibrils (including the NAC domain) has been proposed on the basis of solid-state nuclear magnetic resonance studies, but the atomic structure of the self-assembly of NAC (or AS itself) is still elusive. This is the first study that presents a detailed three-dimensional structure of NAC at atomic resolution. The proposed self-assembled structure of NAC consists of three beta-strands connected by two turn regions. Our study shows that calculated structural parameter values of the simulated fibril-like cross-beta structure of NAC are in excellent agreement with the experimental values. Moreover, the diameter dimensions of the proposed fibril-like structure are also in agreement with experimental measurements. The proposed fibril-like structure of NAC may assist in future work aimed at understanding the formation of aggregates in PD and developing compounds to modulate aggregation.
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