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Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers.

Qiuye LiChristopher P JaroniecWitold K Surewicz
Published in: Nature structural & molecular biology (2022)
One of the least understood aspects of prion diseases is the structure of infectious prion protein aggregates. Here we report a high-resolution cryo-EM structure of amyloid fibrils formed by human prion protein with the Y145Stop mutation that is associated with a familial prion disease. This structural insight allows us not only to explain previous biochemical findings, but also provides direct support for the conformational adaptability model of prion transmissibility barriers.
Keyphrases
  • high resolution
  • endothelial cells
  • early onset
  • molecular dynamics simulations
  • mass spectrometry
  • single molecule
  • small molecule