9HX4
Amyloid fibril of apolipoprotein A-IV
Summary for 9HX4
| Entry DOI | 10.2210/pdb9hx4/pdb |
| EMDB information | 52457 |
| Descriptor | Apolipoprotein A-IV (1 entity in total) |
| Functional Keywords | amyloid, apolipoprotein, fibril, protein fibril |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 10 |
| Total formula weight | 454339.61 |
| Authors | Aibara, S.,Kassner, A.,Wong, E.,Klingel, K.,Papworth, M.,Althage, M.,Wang, Q.D.,Correia, C.,Milting, H.,Oliveira, T.M. (deposition date: 2025-01-06, release date: 2025-11-05) |
| Primary citation | Aibara, S.,Kassner, A.,Wong, E.,Klingel, K.,Papworth, M.,Althage, M.,Wang, Q.D.,Correia, C.,Milting, H.,de Oliveira, T.M. Apolipoprotein A-IV fibrils: structural diagnosis of mixed cardiac amyloidosis. Nat Commun, 16:9276-9276, 2025 Cited by PubMed Abstract: Cardiac amyloidosis (CA) occurs when misfolded proteins deposit as fibrils in the extracellular space of the heart. The fibrillogenic properties of apolipoprotein A-IV (ApoAIV) have been histologically observed and associated with CA pathogenesis. We report the structure of an ApoAIV amyloid from a patient's heart, which coexist amongst transthyretin (TTR) amyloids. These cases of undetected mixed CA highlight the importance of developing broad-spectrum anti-amyloid treatments to improve outcomes in patients. PubMed: 41115976DOI: 10.1038/s41467-025-64902-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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