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TitleStructure of ATTRv-F64S fibrils isolated from skin tissue of a living patient.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Page 781, Year 2025
Publish dateDec 16, 2025
AuthorsJun Yu / Xuefeng Zhang / Sandra Pinton / Elena Vacchi / Andrea Cavalli / Matteo Pecoraro / Giorgia Melli / Andreas Boland /
PubMed AbstractAmyloid 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.
External linksNat Commun / PubMed:41402329 / PubMed Central
MethodsEM (single particle)
Resolution2.8 Å
Structure data

52519

9hyw

EMDB-52519, PDB-9hyw:
Cryo-EM structure of ATTRv-F64S amyloid fibril from patient skin tissue.
Method: EM (single particle) / Resolution: 2.8 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloidosis / amyloid fibrils / ATTR variant / F64S variant

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