Ontology highlight
ABSTRACT:
SUBMITTER: Zhao K
PROVIDER: S-EPMC7250837 | biostudies-literature | 2020 May
REPOSITORIES: biostudies-literature
Zhao Kun K Li Yaowang Y Liu Zhenying Z Long Houfang H Zhao Chunyu C Luo Feng F Sun Yunpeng Y Tao Youqi Y Su Xiao-Dong XD Li Dan D Li Xueming X Liu Cong C
Nature communications 20200526 1
Amyloid aggregation of α-synuclein (α-syn) is closely associated with Parkinson's disease (PD) and other synucleinopathies. Several single amino-acid mutations (e.g. E46K) of α-syn have been identified causative to the early onset of familial PD. Here, we report the cryo-EM structure of an α-syn fibril formed by N-terminally acetylated E46K mutant α-syn (Ac-E46K). The fibril structure represents a distinct fold of α-syn, which demonstrates that the E46K mutation breaks the electrostatic interact ...[more]