9hx4

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'''Unreleased structure'''
 
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The entry 9hx4 is ON HOLD
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==Amyloid fibril of apolipoprotein A-IV==
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<StructureSection load='9hx4' size='340' side='right'caption='[[9hx4]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9hx4]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HX4 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9hx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hx4 OCA], [https://pdbe.org/9hx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hx4 RCSB], [https://www.ebi.ac.uk/pdbsum/9hx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hx4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/APOA4_HUMAN 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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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<ref>PMID:41115976</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9hx4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Aibara S]]
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[[Category: Althage M]]
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[[Category: Correia C]]
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[[Category: Kassner A]]
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[[Category: Klingel K]]
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[[Category: Milting H]]
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[[Category: Oliveira TM]]
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[[Category: Papworth M]]
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[[Category: Wang QD]]
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[[Category: Wong E]]

Current revision

Amyloid fibril of apolipoprotein A-IV

PDB ID 9hx4

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