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TitleCryo-EM structure of disease-related prion fibrils provides insights into seeding barriers.
Journal, issue, pagesNat Struct Mol Biol, Vol. 29, Issue 10, Page 962-965, Year 2022
Publish dateSep 12, 2022
AuthorsQiuye Li / Christopher P Jaroniec / Witold K Surewicz /
PubMed AbstractOne 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 ...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.
External linksNat Struct Mol Biol / PubMed:36097290 / PubMed Central
MethodsEM (helical sym.)
Resolution2.86 - 3.92 Å
Structure data

24514

7rl4

EMDB-24514, PDB-7rl4:
Cryo-EM structure of human PrP23-144 amyloid fibrils
Method: EM (helical sym.) / Resolution: 2.86 Å

27458

8dja

EMDB-27458, PDB-8dja:
Cryo-EM structure of mouse PrP23-144 amyloid fibrils (polymorph 1)
Method: EM (helical sym.) / Resolution: 3.92 Å

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsPROTEIN FIBRIL / Prion / amyloid / moPrP23-144 / prion diseases

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