9R4Z
Murine AA amyloid fibril morphology III (AA III)
Summary for 9R4Z
| Entry DOI | 10.2210/pdb9r4z/pdb |
| EMDB information | 53573 |
| Descriptor | Serum amyloid A-2 protein (1 entity in total) |
| Functional Keywords | amyloid fibril, aa amyloidosis, systemic amyloidosis, aapoaii amyloidosis, misfolfing disease, protein aggregation, protein fibril |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 12 |
| Total formula weight | 139471.55 |
| Authors | Andreotti, G.,Schmidt, M.,Faendrich, M. (deposition date: 2025-05-08, release date: 2025-10-01, Last modification date: 2025-10-08) |
| Primary citation | Andreotti, G.,Higuchi, K.,Schmidt, M.,Fandrich, M. Cryo-EM Observation of AA Amyloid Fibrils in Mouse Model of Systemic AApoAII Amyloidosis. J.Mol.Biol., 437:169438-169438, 2025 Cited by PubMed Abstract: The co-deposition of amyloid fibrils from different precursor proteins is a topic of increasing relevance for protein misfolding diseases. Using cryo-electron microscopy (cryo-EM), we here determined the structures of two serum amyloid A (SAA) protein-derived amyloid fibril morphologies that were extracted from a mouse strain that is primarily known to be associated with apolipoprotein A-II-derived amyloid fibrils. The two fibril morphologies show the same protomer conformation as in previously reported ex vivo amyloid fibrils from SAA protein but a different relative arrangement of fibril protein stacks. These data establish that serum amyloid A-derived amyloid fibrils share the same fibril protein fold in different mouse strains and disease contexts. PubMed: 40945578DOI: 10.1016/j.jmb.2025.169438 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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