6ZCF
Amyloid fibril morphology i (in vitro) from murine SAA1.1 protein
Summary for 6ZCF
| Entry DOI | 10.2210/pdb6zcf/pdb |
| EMDB information | 11162 |
| Descriptor | Serum amyloid A-2 protein (1 entity in total) |
| Functional Keywords | systemic amyloidosis, misfolding disease, inflammation, prion, protein fibril |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 12 |
| Total formula weight | 139471.55 |
| Authors | Bansal, A.,Schmidt, M.,Faendrich, M. (deposition date: 2020-06-11, release date: 2021-02-17, Last modification date: 2024-05-01) |
| Primary citation | Bansal, A.,Schmidt, M.,Rennegarbe, M.,Haupt, C.,Liberta, F.,Stecher, S.,Puscalau-Girtu, I.,Biedermann, A.,Fandrich, M. AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils. Nat Commun, 12:1013-1013, 2021 Cited by PubMed Abstract: Systemic AA amyloidosis is a world-wide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from serum amyloid A (SAA) protein. Using cryo electron microscopy we here show that amyloid fibrils which were purified from AA amyloidotic mice are structurally different from fibrils formed from recombinant SAA protein in vitro. Ex vivo amyloid fibrils consist of fibril proteins that contain more residues within their ordered parts and possess a higher β-sheet content than in vitro fibril proteins. They are also more resistant to proteolysis than their in vitro formed counterparts. These data suggest that pathogenic amyloid fibrils may originate from proteolytic selection, allowing specific fibril morphologies to proliferate and to cause damage to the surrounding tissue. PubMed: 33579941DOI: 10.1038/s41467-021-21129-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.73 Å) |
Structure validation
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