9hx4 | pdb_00009hx4

Amyloid fibril of apolipoprotein A-IV

spinqualitylabelsall models 9hx4, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9hx4 is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function APOA4_HUMAN May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons. Publication Abstract from PubMed 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. Apolipoprotein A-IV fibrils: structural diagnosis of mixed cardiac amyloidosis.,Aibara S, Kassner A, Wong E, Klingel K, Papworth M, Althage M, Wang QD, Correia C, Milting H, de Oliveira TM Nat Commun. 2025 Oct 20;16(1):9276. doi: 10.1038/s41467-025-64902-0. PMID:41115976 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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