ISDA: 9HYW

Deposition Date 2025-01-10

Release Date 2026-01-21

Last Version Date 2026-05-06

Entry Detail

PDB ID:

9HYW

Keywords:

PROTEIN FIBRIL

Title:

Cryo-EM structure of ATTRv-F64S amyloid fibril from patient skin tissue.

Biological Source:

Source Organism(s):

Homo sapiens (Taxon ID: 9606)

Method Details:

Experimental Method:

ELECTRON MICROSCOPY

Resolution:

2.80 Å

Aggregation State:

HELICAL ARRAY

Reconstruction Method:

SINGLE PARTICLE

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Transthyretin
Gene (Uniprot):TTR
Chain IDs:A, B, C, D, E, F, G, H, I
Chain Length:147
Number of Molecules:9
Biological Source:Homo sapiens

UniProt ID:P02766 Pfam ID:PF00576

Ligand Molecules

Primary Citation

Structure of ATTRv-F64S fibrils isolated from skin tissue of a living patient.

Yu, J, Zhang, X, Pinton, S, Vacchi, E, Cavalli, A, Pecoraro, M, Melli, G, Boland, A.Show

Nat Commun 17 781 781 (2025)

PMID: 41402329 DOI: 10.1038/s41467-025-67457-2

Abstact

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.

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Disease

Primary Citation of related structures

Abstact

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