9O8H
amyloid fibril of recombinant full-length 2N4R tau complexed with mouse liver 18S ribosomal RNA
Summary for 9O8H
| Entry DOI | 10.2210/pdb9o8h/pdb |
| Related | 9O8E |
| EMDB information | 70224 70227 |
| Descriptor | Isoform Tau-F of Microtubule-associated protein tau, CHLORIDE ION (2 entities in total) |
| Functional Keywords | amyloid fibril, protein fibril |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 10 |
| Total formula weight | 470264.65 |
| Authors | Jiang, Y.X.,Sawaya, M.R.,Abskharon, R.,Ge, P.,Boyer, D.R.,Eisenberg, D.S. (deposition date: 2025-04-15, release date: 2026-03-18, Last modification date: 2026-05-06) |
| Primary citation | Abskharon, R.,Jiang, Y.X.,Sawaya, M.R.,Ge, P.,Zhang, J.,Boyer, D.R.,Dolinsky, J.L.,Pi, J.,Cascio, D.,Guo, F.,Eisenberg, D.S. Structural evidence that RNA contributes to polymorphism of tau amyloid fibrils. Iscience, 29:115501-115501, 2026 Cited by PubMed Abstract: RNA colocalizes with tau deposits in Alzheimer's disease (AD) and drives tau aggregation . Previously, we determined a cryogenic-electron microscopy (cryo-EM) structure of fibrils of full-length tau bound to unfractionated mammalian RNA, revealing a small tau C-terminal core. Here, we present the cryo-EM structure of fibrils of full-length recombinant tau bound to unfractionated mammalian RNA seeded by AD-extracted tau fibrils. This structure reveals an expanded tau C-terminal core resembling AD tau fibrils. RNA sequencing identified 18S ribosomal RNA as the primary fibril-bound species. Next, we determined the cryo-EM structure of fibrils of full-length recombinant tau bound to mammalian 18S ribosomal RNA, revealing a core that consists of the R2 to R4 repeat domains previously seen in pathological tau fibrils. All our recombinant RNA-tau fibrils dissolve upon RNase treatment. Tau fibrils adopt distinct folds in the presence of different RNAs, suggesting RNA is a cofactor capable of shaping tau fibril polymorphism. PubMed: 42006351DOI: 10.1016/j.isci.2026.115501 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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