9CDA
Structure of type I-2 alpha-synuclein filament from multiple system atrophy
Summary for 9CDA
| Entry DOI | 10.2210/pdb9cda/pdb |
| Related | 9CD9 |
| EMDB information | 45464 45465 |
| Descriptor | Alpha-synuclein (1 entity in total) |
| Functional Keywords | fibril, synuclein, protein fibril |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 18 |
| Total formula weight | 260569.94 |
| Authors | Yan, N.L.,Candido, F.,Tse, E.,Melo, A.A.,Southworth, D.R.,Merz, G.E. (deposition date: 2024-06-24, release date: 2024-11-27, Last modification date: 2025-01-22) |
| Primary citation | Yan, N.L.,Candido, F.,Tse, E.,Melo, A.A.,Prusiner, S.B.,Mordes, D.A.,Southworth, D.R.,Paras, N.A.,Merz, G.E. Cryo-EM structure of a novel alpha-synuclein filament subtype from multiple system atrophy. Febs Lett., 599:33-40, 2025 Cited by PubMed Abstract: Multiple system atrophy (MSA) is a progressive neurodegenerative disease characterized by accumulation of α-synuclein cross-β amyloid filaments in the brain. Previous structural studies of these filaments by cryo-electron microscopy (cryo-EM) revealed three discrete folds distinct from α-synuclein filaments associated with other neurodegenerative diseases. Here, we use cryo-EM to identify a novel, low-populated MSA filament subtype (designated Type I) in addition to a predominant class comprising MSA Type II filaments. The 3.3-Å resolution structure of the Type I filament reveals a fold consisting of two asymmetric protofilaments, one of which adopts a novel structure that is chimeric between two previously reported protofilaments. These results further define MSA-specific folds of α-synuclein filaments and have implications for designing MSA diagnostics and therapeutics. PubMed: 39511911DOI: 10.1002/1873-3468.15048 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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