9HYW
Cryo-EM structure of ATTRv-F64S amyloid fibril from patient skin tissue.
Summary for 9HYW
| Entry DOI | 10.2210/pdb9hyw/pdb |
| EMDB information | 52519 |
| Descriptor | Transthyretin (1 entity in total) |
| Functional Keywords | amyloidosis, amyloid fibrils, attr variant, f64s variant, protein fibril |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 9 |
| Total formula weight | 142603.98 |
| Authors | Yu, J.,Zhang, X.,Boland, A. (deposition date: 2025-01-10, release date: 2026-01-21, Last modification date: 2026-05-06) |
| Primary citation | Yu, J.,Zhang, X.,Pinton, S.,Vacchi, E.,Cavalli, A.,Pecoraro, M.,Melli, G.,Boland, A. Structure of ATTRv-F64S fibrils isolated from skin tissue of a living patient. Nat Commun, 17:781-781, 2025 Cited by PubMed Abstract: Amyloid transthyretin-derived (ATTR) amyloidosis is a degenerative, systemic disease characterized by transthyretin fibril deposition in organs like the heart, kidneys, liver, and skin. In this study, we report the cryo-EM structure of transthyretin fibrils isolated from skin tissue of a living patient carrying a rare genetic mutation (ATTRv F64S). The structure adopts a highly conserved fold previously observed in other ATTR fibrils from various tissues or different genetic variants. Mass spectrometry was used to evaluate fibril content and to identify common post-translational modifications. The structural consistency between ATTR filaments from different tissues or patients validates non-invasive skin biopsy as a diagnostic tool. PubMed: 41402329DOI: 10.1038/s41467-025-67457-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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