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-Structure paper
Title | Light chain mutations contribute to defining the fibril morphology in systemic AL amyloidosis. |
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Journal, issue, pages | Nat Commun, Vol. 15, Issue 1, Page 5121, Year 2024 |
Publish date | Jun 15, 2024 |
![]() | Sara Karimi-Farsijani / Peter Benedikt Pfeiffer / Sambhasan Banerjee / Julian Baur / Lukas Kuhn / Niklas Kupfer / Ute Hegenbart / Stefan O Schönland / Sebastian Wiese / Christian Haupt / Matthias Schmidt / Marcus Fändrich / ![]() |
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 ...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. |
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Methods | EM (helical sym.) |
Resolution | 2.25 - 2.92 Å |
Structure data | EMDB-18881, PDB-8r47: EMDB-19818, PDB-9eme: |
Source |
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![]() | PROTEIN FIBRIL / Amyloid fibril / AL amyloid |