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TitleCryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 3609, Year 2018
Publish dateSep 6, 2018
AuthorsBinsen Li / Peng Ge / Kevin A Murray / Phorum Sheth / Meng Zhang / Gayatri Nair / Michael R Sawaya / Woo Shik Shin / David R Boyer / Shulin Ye / David S Eisenberg / Z Hong Zhou / Lin Jiang /
PubMed Abstractα-Synuclein (aSyn) fibrillar polymorphs have distinct in vitro and in vivo seeding activities, contributing differently to synucleinopathies. Despite numerous prior attempts, how polymorphic aSyn ...α-Synuclein (aSyn) fibrillar polymorphs have distinct in vitro and in vivo seeding activities, contributing differently to synucleinopathies. Despite numerous prior attempts, how polymorphic aSyn fibrils differ in atomic structure remains elusive. Here, we present fibril polymorphs from the full-length recombinant human aSyn and their seeding capacity and cytotoxicity in vitro. By cryo-electron microscopy helical reconstruction, we determine the structures of the two predominant species, a rod and a twister, both at 3.7 Å resolution. Our atomic models reveal that both polymorphs share a kernel structure of a bent β-arch, but differ in their inter-protofilament interfaces. Thus, different packing of the same kernel structure gives rise to distinct fibril polymorphs. Analyses of disease-related familial mutations suggest their potential contribution to the pathogenesis of synucleinopathies by altering population distribution of the fibril polymorphs. Drug design targeting amyloid fibrils in neurodegenerative diseases should consider the formation and distribution of concurrent fibril polymorphs.
External linksNat Commun / PubMed:30190461 / PubMed Central
MethodsEM (helical sym.)
Resolution3.5 - 3.6 Å
Structure data

EMDB-7618, PDB-6cu7:
Alpha Synuclein fibril formed by full length protein - Rod Polymorph
Method: EM (helical sym.) / Resolution: 3.5 Å

EMDB-7619, PDB-6cu8:
Alpha Synuclein fibril formed by full length protein - Twister Polymorph
Method: EM (helical sym.) / Resolution: 3.6 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Parkinson's disease / Synucleinopathy / Amyloid aggregation / Fibril polymorphism

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