Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion.

doi:10.1038/s41467-022-31240-4

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Article

Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion.

Nature communications - 17 Jun 2022

Wang Li-Qiang, Ma Yeyang, Yuan Han-Ye, Zhao Kun, Zhang Mu-Ya, Wang Qiang, Huang Xi, Xu Wen-Chang, Dai Bin, Chen Jie, Li Dan, Zhang Delin, Wang Zhengzhi, Zou Liangyu, Yin Ping, Liu Cong, Liang Yi

Abstract excerpt

Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease. Misfolded Cu, Zn-superoxide dismutase (SOD1) has been linked to both familial and sporadic ALS. SOD1 fibrils formed in vitro share toxic properties with ALS inclusions. Here we produced cytotoxic amyloid fibrils from full-length apo human SOD1 under reducing conditions and determined the atomic structure using cryo-EM. The SOD1 fibril consists of...

Topics

Amyloid
Amyotrophic Lateral Sclerosis
Cryoelectron Microscopy
Humans
Mutation
Superoxide Dismutase-1

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Identifiers

PMID: 35715417
DOI: 10.1038/s41467-022-31240-4
PMCID: PMC9205981

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