8R47

AL amyloid fibril from the FOR010 light chain

Summary for 8R47

• Entry DOI: 10.2210/pdb8r47/pdb
• EMDB information: 18881
• Descriptor: lambda 3 immunoglobulin light chain fragment, residues 4-116 (1 entity in total)
• Functional Keywords: amyloid fibril, al amyloid, protein fibril
• Biological source: Homo sapiens
• Total number of polymer chains: 6
• Total formula weight: 72380.02

Authors

Pfeiffer, P.B.,Banerjee, S.,Schmidt, M.,Faendrich, M. (deposition date: 2023-11-13, release date: 2024-06-26, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (2.25 Å)