7LNA
Infectious mammalian prion fibril (263K scrapie)
Summary for 7LNA
| Entry DOI | 10.2210/pdb7lna/pdb |
| EMDB information | 23459 |
| Descriptor | Major prion protein (1 entity in total) |
| Functional Keywords | infectious mammalian prion, templating, glycosylated glycophophatidlyinositol-anchored amyloid, piribs, protein fibril |
| Biological source | Mesocricetus auratus (Golden hamster) |
| Total number of polymer chains | 3 |
| Total formula weight | 48792.30 |
| Authors | Kraus, A.,Hoyt, F.,Schwartz, C.L.,Hansen, B.,Hughson, A.G.,Artikis, E.,Race, B.,Caughey, B. (deposition date: 2021-02-06, release date: 2021-09-01, Last modification date: 2024-11-06) |
| Primary citation | Kraus, A.,Hoyt, F.,Schwartz, C.L.,Hansen, B.,Artikis, E.,Hughson, A.G.,Raymond, G.J.,Race, B.,Baron, G.S.,Caughey, B. High-resolution structure and strain comparison of infectious mammalian prions. Mol.Cell, 81:4540-, 2021 Cited by PubMed Abstract: Within the extensive range of self-propagating pathologic protein aggregates of mammals, prions are the most clearly infectious (e.g., ∼10 lethal doses per milligram). The structures of such lethal assemblies of PrP molecules have been poorly understood. Here we report a near-atomic core structure of a brain-derived, fully infectious prion (263K strain). Cryo-electron microscopy showed amyloid fibrils assembled with parallel in-register intermolecular β sheets. Each monomer provides one rung of the ordered fibril core, with N-linked glycans and glycolipid anchors projecting outward. Thus, single monomers form the templating surface for incoming monomers at fibril ends, where prion growth occurs. Comparison to another prion strain (aRML) revealed major differences in fibril morphology but, like 263K, an asymmetric fibril cross-section without paired protofilaments. These findings provide structural insights into prion propagation, strains, species barriers, and membrane pathogenesis. This structure also helps frame considerations of factors influencing the relative transmissibility of other pathologic amyloids. PubMed: 34433091DOI: 10.1016/j.molcel.2021.08.011 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.14 Å) |
Structure validation
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