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-Structure paper
Title | Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 29, Issue 10, Page 962-965, Year 2022 |
Publish date | Sep 12, 2022 |
Authors | Qiuye Li / Christopher P Jaroniec / Witold K Surewicz / |
PubMed Abstract | 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 ...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 links | Nat Struct Mol Biol / PubMed:36097290 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 2.86 - 3.92 Å |
Structure data | EMDB-24514, PDB-7rl4: EMDB-27458, PDB-8dja: |
Source |
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Keywords | PROTEIN FIBRIL / Prion / amyloid / moPrP23-144 / prion diseases |