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

  • Marcus Gallagher-Jones
  • , Calina Glynn
  • , David R. Boyer
  • , Michael W. Martynowycz
  • , Evelyn Hernandez
  • , Jennifer Miao
  • , Chih Te Zee
  • , Irina V. Novikova
  • , Lukasz Goldschmidt
  • , Heather T. McFarlane
  • , Gustavo F. Helguera
  • , James E. Evans
  • , Michael R. Sawaya
  • , Duilio Cascio
  • , David S. Eisenberg
  • , Tamir Gonen
  • , Jose A. Rodriguez
  • University of California
  • University of California at Los Angeles
  • Environmental Molecular Sciences Laboratory
  • Laboratorio de Biologia Del Comportamiento
  • Howard Hughes Medical Institute

Research output: Contribution to journalArticlepeer-review

76 Scopus citations

Abstract

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'.

Original languageEnglish
Pages (from-to)131-134
Number of pages4
JournalNature Structural and Molecular Biology
Volume25
Issue number2
DOIs
StatePublished - Feb 1 2018

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