9HX3

Amyloid fibril of TTR

Summary for 9HX3

Entry DOI	10.2210/pdb9hx3/pdb
EMDB information	52456
Descriptor	Transthyretin (1 entity in total)
Functional Keywords	amyloid, fibril, transthyretin, protein fibril
Biological source	Homo sapiens (human)
Total number of polymer chains	5
Total formula weight	79524.92
Authors	Aibara, S.,Kassner, E.,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: 41115976 DOI: 10.1038/s41467-025-64902-0 PDB entries with the same primary citation
Experimental method	ELECTRON MICROSCOPY (3 Å)

Structure validation