Summary for 6H6B
| Entry DOI | 10.2210/pdb6h6b/pdb |
| EMDB information | 0148 |
| Descriptor | Alpha-synuclein (1 entity in total) |
| Functional Keywords | parkinson's disease, apha-synuclein, fibril, filament, protein fibril |
| Biological source | Homo sapiens |
| Total number of polymer chains | 10 |
| Total formula weight | 122428.73 |
| Authors | Guerrero-Ferreira, R.,Taylor, N.M.I.,Mona, D.,Ringler, P.,Lauer, M.E.,Riek, R.,Britschgi, M.,Stahlberg, H. (deposition date: 2018-07-26, release date: 2018-08-08, Last modification date: 2024-07-10) |
| Primary citation | Guerrero-Ferreira, R.,Taylor, N.M.,Mona, D.,Ringler, P.,Lauer, M.E.,Riek, R.,Britschgi, M.,Stahlberg, H. Cryo-EM structure of alpha-synuclein fibrils. Elife, 7:-, 2018 Cited by PubMed Abstract: Parkinson's disease is a progressive neuropathological disorder that belongs to the class of synucleinopathies, in which the protein alpha-synuclein is found at abnormally high concentrations in affected neurons. Its hallmark are intracellular inclusions called Lewy bodies and Lewy neurites. We here report the structure of cytotoxic alpha-synuclein fibrils (residues 1-121), determined by cryo-electron microscopy at a resolution of 3.4 Å. Two protofilaments form a polar fibril composed of staggered β-strands. The backbone of residues 38 to 95, including the fibril core and the non-amyloid component region, are well resolved in the EM map. Residues 50-57, containing three of the mutation sites associated with familial synucleinopathies, form the interface between the two protofilaments and contribute to fibril stability. A hydrophobic cleft at one end of the fibril may have implications for fibril elongation, and invites for the design of molecules for diagnosis and treatment of synucleinopathies. PubMed: 29969391DOI: 10.7554/eLife.36402 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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