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-Structure paper
| タイトル | Structure of ATTRv-F64S fibrils isolated from skin tissue of a living patient. |
|---|---|
| ジャーナル・号・ページ | Nat Commun, Vol. 17, Issue 1, Page 781, Year 2025 |
| 掲載日 | 2025年12月16日 |
著者 | Jun Yu / Xuefeng Zhang / Sandra Pinton / Elena Vacchi / Andrea Cavalli / Matteo Pecoraro / Giorgia Melli / Andreas Boland / ![]() |
| PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:41402329 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.8 Å |
| 構造データ | EMDB-52519, PDB-9hyw: |
| 由来 |
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キーワード | PROTEIN FIBRIL / amyloidosis / amyloid fibrils / ATTR variant / F64S variant |
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homo sapiens (ヒト)
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