5L6Q

Refolded AL protein from cardiac amyloidosis

Summary for 5L6Q

• Entry DOI: 10.2210/pdb5l6q/pdb
• Related: 4OD2
• Descriptor: H5AL, ZINC ION, SODIUM ION, ... (8 entities in total)
• Functional Keywords: antibody, light chain, systemic al amyloidosis, amyloid fibrils, immune system
• Biological source: Homo sapiens
• Total number of polymer chains: 2
• Total formula weight: 25213.06

Authors

Annamalai, K.,Liberta, F.,Vielberg, M.-T.,Lilie, H.,Guehrs, K.-H.,Schierhorn, A.,Koehler, R.,Schmidt, A.,Haupt, C.,Hegenbart, O.,Schoenland, S.,Groll, M.,Faendrich, M. (deposition date: 2016-05-31, release date: 2017-05-31, Last modification date: 2024-10-09)

Primary citation

Annamalai, K.,Liberta, F.,Vielberg, M.T.,Close, W.,Lilie, H.,Guhrs, K.H.,Schierhorn, A.,Koehler, R.,Schmidt, A.,Haupt, C.,Hegenbart, U.,Schonland, S.,Schmidt, M.,Groll, M.,Fandrich, M.
Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo.
Angew. Chem. Int. Ed. Engl., 56:7510-7514, 2017

PubMed Abstract: Systemic amyloidosis is caused by the misfolding of a circulating amyloid precursor protein and the deposition of amyloid fibrils in multiple organs. Chemical and biophysical analysis of amyloid fibrils from human AL and murine AA amyloidosis reveal the same fibril morphologies in different tissues or organs of one patient or diseased animal. The observed structural similarities concerned the fibril morphology, the fibril protein primary and secondary structures, the presence of post-translational modifications and, in case of the AL fibrils, the partially folded characteristics of the polypeptide chain within the fibril. Our data imply for both analyzed forms of amyloidosis that the pathways of protein misfolding are systemically conserved; that is, they follow the same rules irrespective of where inside one body fibrils are formed or accumulated.

PubMed: 28544119
DOI: 10.1002/anie.201701761

Experimental method

X-RAY DIFFRACTION (1.4 Å)