8cpe

CryoEM structure of AL55 amyloid fibrils extracted from the kidney of an AL amyloidosis patient.

spinqualitylabelsall models 8cpe, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8cpe is a 5 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 4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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