| Literature DB >> 29633780 |
Matteo Rovere1, John B Sanderson1, Luis Fonseca-Ornelas1, Dushyant S Patel1, Tim Bartels1.
Abstract
α-Synuclein (αSyn) is a key player in the pathogenesis of Parkinson's disease and other synucleinopathies. Here, we report the existence of a novel soluble α-helical conformer of αSyn, obtained through transient interaction with lipid interfaces, and propose dynamic oligomerization as the mechanism underlying its stability. The conformational space of αSyn appears to be highly context-dependent, and lipid bilayers might thus play crucial roles as molecular chaperones in a cellular environment.Entities:
Keywords: Parkinson's disease; intrinsically disordered proteins; protein folding; small unilamellar vesicles; α-synuclein
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Year: 2018 PMID: 29633780 DOI: 10.1002/1873-3468.13047
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124