8CPE

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

Summary for 8CPE

• Entry DOI: 10.2210/pdb8cpe/pdb
• Related: 6HUD
• EMDB information: 0274 16780
• Descriptor: Immunoglobulin lambda light chain (1 entity in total)
• Functional Keywords: light chains, amyloid fibrils, al amyloidosis., protein fibril
• Biological source: Homo sapiens
• Total number of polymer chains: 5
• Total formula weight: 116632.79

Authors

Puri, S.,Schulte, T.,Chaves-Sanjuan, A.,Ricagno, S. (deposition date: 2023-03-02, release date: 2023-08-16, Last modification date: 2024-11-06)

Primary citation

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.
The Cryo-EM STRUCTURE of Renal Amyloid Fibril Suggests Structurally Homogeneous Multiorgan Aggregation in AL Amyloidosis.
J.Mol.Biol., 435:168215-168215, 2023

PubMed Abstract: 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 Å 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.

PubMed: 37516426
DOI: 10.1016/j.jmb.2023.168215

Experimental method

ELECTRON MICROSCOPY (4 Å)