6SHS
Abeta fibril (Morphology I)
Summary for 6SHS
| Entry DOI | 10.2210/pdb6shs/pdb |
| EMDB information | 10204 4864 4866 |
| Descriptor | Amyloid-beta precursor protein (1 entity in total) |
| Functional Keywords | fibril, beta amyloid, cryo-em, protein fibril |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 12 |
| Total formula weight | 52030.22 |
| Authors | Kollmer, M.,Fandrich, M. (deposition date: 2019-08-08, release date: 2019-11-06, Last modification date: 2024-05-22) |
| Primary citation | Kollmer, M.,Close, W.,Funk, L.,Rasmussen, J.,Bsoul, A.,Schierhorn, A.,Schmidt, M.,Sigurdson, C.J.,Jucker, M.,Fandrich, M. Cryo-EM structure and polymorphism of A beta amyloid fibrils purified from Alzheimer's brain tissue. Nat Commun, 10:4760-4760, 2019 Cited by PubMed Abstract: The formation of Aβ amyloid fibrils is a neuropathological hallmark of Alzheimer's disease and cerebral amyloid angiopathy. However, the structure of Aβ amyloid fibrils from brain tissue is poorly understood. Here we report the purification of Aβ amyloid fibrils from meningeal Alzheimer's brain tissue and their structural analysis with cryo-electron microscopy. We show that these fibrils are polymorphic but consist of similarly structured protofilaments. Brain derived Aβ amyloid fibrils are right-hand twisted and their peptide fold differs sharply from previously analyzed Aβ fibrils that were formed in vitro. These data underscore the importance to use patient-derived amyloid fibrils when investigating the structural basis of the disease. PubMed: 31664019DOI: 10.1038/s41467-019-12683-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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