8CPE

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

8CPE の概要

• エントリーDOI: 10.2210/pdb8cpe/pdb
• 関連するPDBエントリー: 6HUD
• EMDBエントリー: 0274 16780
• 分子名称: Immunoglobulin lambda light chain (1 entity in total)
• 機能のキーワード: light chains, amyloid fibrils, al amyloidosis., protein fibril
• 由来する生物種: Homo sapiens
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 116632.79

構造登録者

Puri, S.,Schulte, T.,Chaves-Sanjuan, A.,Ricagno, S. (登録日: 2023-03-02, 公開日: 2023-08-16, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (4 Å)