8SEH
PHF Tau from Down Syndrome
Summary for 8SEH
Entry DOI | 10.2210/pdb8seh/pdb |
EMDB information | 40411 |
Descriptor | Microtubule-associated protein tau (1 entity in total) |
Functional Keywords | phf tau, tau filament, down syndrome, neuropeptide, human trisomy 21 |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 10 |
Total formula weight | 79401.41 |
Authors | Hoq, M.R.,Bharath, S.R.,Jiang, W.,Vago, F.S. (deposition date: 2023-04-10, release date: 2024-04-03, Last modification date: 2024-06-26) |
Primary citation | Fernandez, A.,Hoq, M.R.,Hallinan, G.I.,Li, D.,Bharath, S.R.,Vago, F.S.,Zhang, X.,Ozcan, K.A.,Newell, K.L.,Garringer, H.J.,Jiang, W.,Ghetti, B.,Vidal, R. Cryo-EM structures of amyloid-beta and tau filaments in Down syndrome. Nat.Struct.Mol.Biol., 31:903-909, 2024 Cited by PubMed Abstract: Adult individuals with Down syndrome (DS) develop Alzheimer disease (AD). Whether there is a difference between AD in DS and AD regarding the structure of amyloid-β (Aβ) and tau filaments is unknown. Here we report the structure of Aβ and tau filaments from two DS brains. We found two Aβ filaments (types IIIa and IIIb) that differ from those previously reported in sporadic AD and two types of Aβ filaments (I and II) identical to those found in sporadic and familial AD. Tau filaments (paired helical filaments and straight filaments) were identical to those in AD, supporting the notion of a common mechanism through which amyloids trigger aggregation of tau. This knowledge is important for understanding AD in DS and assessing whether adults with DS could be included in AD clinical trials. PubMed: 38553642DOI: 10.1038/s41594-024-01252-3 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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