View source for 8cpe


==CryoEM structure of AL55 amyloid fibrils extracted from the kidney of an AL amyloidosis patient.==
<StructureSection load='8cpe' size='340' side='right'caption='[[8cpe]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8cpe]] is a 5 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=8CPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CPE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8cpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cpe OCA], [https://pdbe.org/8cpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cpe RCSB], [https://www.ebi.ac.uk/pdbsum/8cpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cpe ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Immunoglobulin light chain amyloidosis (AL) is caused by the aberrant production of amyloidogenic light chains (LC) that accumulate as amyloid deposits in vital organs. Distinct LC sequences in each patient yield distinct amyloid structures. However different tissue microenvironments may also cause identical protein precursors to adopt distinct amyloid structures. To address the impact of the tissue environment on the structural polymorphism of amyloids, we extracted fibrils from the kidney of an AL patient (AL55) whose cardiac amyloid structure was previously determined by our group. Here we show that the 4.0 A resolution cryo-EM structure of the renal fibril is virtually identical to that reported for the cardiac fibril. These results provide the first structural evidence that LC amyloids independently deposited in different organs of the same AL patient share a common fold.

The Cryo-EM STRUCTURE of Renal Amyloid Fibril Suggests Structurally Homogeneous Multiorgan Aggregation in AL Amyloidosis.,Puri S, Schulte T, Chaves-Sanjuan A, Mazzini G, Caminito S, Pappone C, Anastasia L, Milani P, Merlini G, Bolognesi M, Nuvolone M, Palladini G, Ricagno S J Mol Biol. 2023 Sep 15;435(18):168215. doi: 10.1016/j.jmb.2023.168215. Epub 2023 , Jul 27. PMID:37516426<ref>PMID:37516426</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 8cpe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chaves-Sanjuan A]]
[[Category: Puri S]]
[[Category: Ricagno S]]
[[Category: Schulte T]]