8R47

AL amyloid fibril from the FOR010 light chain

8R47 の概要

• エントリーDOI: 10.2210/pdb8r47/pdb
• EMDBエントリー: 18881
• 分子名称: lambda 3 immunoglobulin light chain fragment, residues 4-116 (1 entity in total)
• 機能のキーワード: amyloid fibril, al amyloid, protein fibril
• 由来する生物種: Homo sapiens
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 72380.02

構造登録者

Pfeiffer, P.B.,Banerjee, S.,Schmidt, M.,Faendrich, M. (登録日: 2023-11-13, 公開日: 2024-06-26, 最終更新日: 2024-10-23)

主引用文献

Karimi-Farsijani, S.,Pfeiffer, P.B.,Banerjee, S.,Baur, J.,Kuhn, L.,Kupfer, N.,Hegenbart, U.,Schonland, S.O.,Wiese, S.,Haupt, C.,Schmidt, M.,Fandrich, M.
Light chain mutations contribute to defining the fibril morphology in systemic AL amyloidosis.
Nat Commun, 15:5121-5121, 2024

PubMed Abstract: Systemic AL amyloidosis is one of the most frequently diagnosed forms of systemic amyloidosis. It arises from mutational changes in immunoglobulin light chains. To explore whether these mutations may affect the structure of the formed fibrils, we determine and compare the fibril structures from several patients with cardiac AL amyloidosis. All patients are affected by light chains that contain an IGLV3-19 gene segment, and the deposited fibrils differ by the mutations within this common germ line background. Using cryo-electron microscopy, we here find different fibril structures in each patient. These data establish that the mutations of amyloidogenic light chains contribute to defining the fibril architecture and hence the structure of the pathogenic agent.

PubMed: 38879609
DOI: 10.1038/s41467-024-49520-6

実験手法

ELECTRON MICROSCOPY (2.25 Å)