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Wang, Li-Qiang; Zhao, Kun; Yuan, Han-Ye; Wang, Qiang; Guan, Zeyuan; Tao, Jing; Li, Xiang-Ning; Sun, Yunpeng; Yi, Chuan-Wei; Chen, Jie; Li, Dan; Zhang, Delin; Yin, Ping; Liu, Cong; Liang, Yi
Nature structural & molecular biology, 06/2020, Letnik: 27, Številka: 6Journal Article
Prion diseases are caused by the misfolding of prion protein (PrP). Misfolded PrP forms protease-resistant aggregates in vivo (PrP ) that are able to template the conversion of the native form of the protein (PrP ), a property shared by in vitro-produced PrP fibrils. Here we produced amyloid fibrils in vitro from recombinant, full-length human PrP (residues 23-231) and determined their structure using cryo-EM, building a model for the fibril core comprising residues 170-229. The PrP fibril consists of two protofibrils intertwined in a left-handed helix. Lys194 and Glu196 from opposing subunits form salt bridges, creating a hydrophilic cavity at the interface of the two protofibrils. By comparison with the structure of PrP , we propose that two α-helices in the C-terminal domain of PrP are converted into β-strands stabilized by a disulfide bond in the PrP fibril. Our data suggest that different PrP mutations may play distinct roles in modulating the conformational conversion.
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