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Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp.

Nat. Struct. Mol. Biol.. 2018-02; 
Gallagher-JonesMarcus,GlynnCalina,BoyerDavid R,MartynowyczMichael W,HernandezEvelyn,MiaoJennifer,ZeeChih-Te,NovikovaIrina V,GoldschmidtLukasz,McFarlaneHeather T,HelgueraGustavo F,EvansJames E,SawayaMichael R,CascioDuilio,EisenbergDavid S,GonenTamir,RodriguezJo
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Peptide Synthesis … were selected and aligned. Characterization of proto-PrP Sc peptide. The synthetic peptide, QYNNQNNFV, corresponding to residues 168–176 of the bank vole prion protein was purchased from GenScript. The peptide used … Get A Quote

摘要

The atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-ångström-resolution structure of a protofibril formed by a wild-type segment from the β2-α2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named 'polar clasps'.

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