8A00
Infectious mouse-adapted ME7 scrapie prion fibril purified from terminally-infected mouse brains
Summary for 8A00
| Entry DOI | 10.2210/pdb8a00/pdb |
| EMDB information | 15043 |
| Descriptor | Major prion protein (1 entity in total) |
| Functional Keywords | prion, protein fibril |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 3 |
| Total formula weight | 47329.89 |
| Authors | Manka, S.W.,Wenborn, A.,Betts, J.,Joiner, S.,Saibil, H.R.,Collinge, J.,Wadsworth, J.D.F. (deposition date: 2022-05-26, release date: 2023-01-18, Last modification date: 2023-05-10) |
| Primary citation | Manka, S.W.,Wenborn, A.,Betts, J.,Joiner, S.,Saibil, H.R.,Collinge, J.,Wadsworth, J.D.F. A structural basis for prion strain diversity. Nat.Chem.Biol., 19:607-613, 2023 Cited by PubMed Abstract: Recent cryogenic electron microscopy (cryo-EM) studies of infectious, ex vivo, prion fibrils from hamster 263K and mouse RML prion strains revealed a similar, parallel in-register intermolecular β-sheet (PIRIBS) amyloid architecture. Rungs of the fibrils are composed of individual prion protein (PrP) monomers that fold to create distinct N-terminal and C-terminal lobes. However, disparity in the hamster/mouse PrP sequence precludes understanding of how divergent prion strains emerge from an identical PrP substrate. In this study, we determined the near-atomic resolution cryo-EM structure of infectious, ex vivo mouse prion fibrils from the ME7 prion strain and compared this with the RML fibril structure. This structural comparison of two biologically distinct mouse-adapted prion strains suggests defined folding subdomains of PrP rungs and the way in which they are interrelated, providing a structural definition of intra-species prion strain-specific conformations. PubMed: 36646960DOI: 10.1038/s41589-022-01229-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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