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| Title | Cryo-EM observation of the amyloid key structure of polymorphic TDP-43 amyloid fibrils. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 15, Issue 1, Page 486, Year 2024 |
| Publish date | Jan 12, 2024 |
 Authors | Kartikay Sharma / Fabian Stockert / Jayakrishna Shenoy / Mélanie Berbon / Muhammed Bilal Abdul-Shukkoor / Birgit Habenstein / Antoine Loquet / Matthias Schmidt / Marcus Fändrich /   |
| PubMed Abstract | The transactive response DNA-binding protein-43 (TDP-43) is a multi-facet protein involved in phase separation, RNA-binding, and alternative splicing. In the context of neurodegenerative diseases, ...The transactive response DNA-binding protein-43 (TDP-43) is a multi-facet protein involved in phase separation, RNA-binding, and alternative splicing. In the context of neurodegenerative diseases, abnormal aggregation of TDP-43 has been linked to amyotrophic lateral sclerosis and frontotemporal lobar degeneration through the aggregation of its C-terminal domain. Here, we report a cryo-electron microscopy (cryo-EM)-based structural characterization of TDP-43 fibrils obtained from the full-length protein. We find that the fibrils are polymorphic and contain three different amyloid structures. The structures differ in the number and relative orientation of the protofilaments, although they share a similar fold containing an amyloid key motif. The observed fibril structures differ from previously described conformations of TDP-43 fibrils and help to better understand the structural landscape of the amyloid fibril structures derived from this protein. |
 External links | Nat Commun / PubMed:38212334 / PubMed Central |
| Methods | EM (helical sym.) |
| Resolution | 3.76 - 4.05 Å |
| Structure data | EMDB-18715, PDB-8qx9: EMDB-18716, PDB-8qxa: EMDB-18717, PDB-8qxb: |
| Source |
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 Keywords | PROTEIN FIBRIL /  Amyloidosis / Protein misfolding disease / Amyloid fibrils / Cryo electron microscopy / Amyloid key |
