6z1o

AL amyloid fibril from a lambda 3 light chain in conformation A

spinqualitylabelsall models 6z1o, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Systemic AL amyloidosis is a debilitating and potentially fatal disease that arises from the misfolding and fibrillation of immunoglobulin light chains (LCs). The disease is patient-specific with essentially each patient possessing a unique LC sequence. In this study, we present two ex vivo fibril structures of a lambda3 LC. The fibrils were extracted from the explanted heart of a patient (FOR005) and consist of 115-residue fibril proteins, mainly from the LC variable domain. The fibril structures imply that a 180 degrees rotation around the disulfide bond and a major unfolding step are necessary for fibrils to form. The two fibril structures show highly similar fibril protein folds, differing in only a 12-residue segment. Remarkably, the two structures do not represent separate fibril morphologies, as they can co-exist at different z-axial positions within the same fibril. Our data imply the presence of structural breaks at the interface of the two structural forms. Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis.,Radamaker L, Baur J, Huhn S, Haupt C, Hegenbart U, Schonland S, Bansal A, Schmidt M, Fandrich M Nat Commun. 2021 Feb 8;12(1):875. doi: 10.1038/s41467-021-21126-2. PMID:33558536 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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