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- PDB-29os: AD fold in mouse injected with seeds of AD -

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Basic information

Entry
Database: PDB / ID: 29os
TitleAD fold in mouse injected with seeds of AD
ComponentsIsoform Tau-A of Microtubule-associated protein tau
KeywordsSTRUCTURAL PROTEIN / Amyloid / prion / tau / Alzheimer's Disease.
Function / homology
Function and homology information


negative regulation of tubulin deacetylation / Caspase-mediated cleavage of cytoskeletal proteins / negative regulation of intracellular transport / positive regulation of mesenchymal stem cell migration / positive regulation of long-term synaptic depression / PKR-mediated signaling / axon extension / adult walking behavior / mRNA transport / intrinsic apoptotic signaling pathway in response to oxidative stress ...negative regulation of tubulin deacetylation / Caspase-mediated cleavage of cytoskeletal proteins / negative regulation of intracellular transport / positive regulation of mesenchymal stem cell migration / positive regulation of long-term synaptic depression / PKR-mediated signaling / axon extension / adult walking behavior / mRNA transport / intrinsic apoptotic signaling pathway in response to oxidative stress / axo-dendritic transport / mitochondrion transport along microtubule / positive regulation of mitochondrial membrane potential / microtubule stabilizing activity / neurofibrillary tangle / microtubule lateral binding / tubulin complex / positive regulation of protein localization to synapse / regulation of microtubule-based movement / negative regulation of protein localization to mitochondrion / intracellular distribution of mitochondria / lipoprotein particle binding / negative regulation of mitochondrial membrane potential / microtubule polymerization / response to hyperoxia / apolipoprotein binding / regulation of calcium-mediated signaling / main axon / glial cell projection / regulation of microtubule polymerization or depolymerization / axoneme / axonal growth cone / negative regulation of mitochondrial fission / protein polymerization / positive regulation of axon extension / axolemma / regulation of cellular response to heat / positive regulation of microtubule polymerization / axonogenesis / heat shock protein binding / positive regulation of superoxide anion generation / positive regulation of protein localization / supramolecular fiber organization / synapse assembly / somatodendritic compartment / response to nutrient / nuclear periphery / protein phosphatase 2A binding / enzyme inhibitor activity / positive regulation of neuron projection development / SH3 domain binding / neuron migration / regulation of microtubule cytoskeleton organization / microtubule cytoskeleton organization / memory / Hsp90 protein binding / regulation of autophagy / protein homooligomerization / synapse organization / response to lead ion / neuron projection development / cytoplasmic ribonucleoprotein granule / microtubule cytoskeleton / microtubule / protein-folding chaperone binding / growth cone / cell body / microtubule binding / amyloid fibril formation / cytoplasmic side of plasma membrane / learning or memory / postsynaptic density / membrane raft / negative regulation of gene expression / axon / neuronal cell body / DNA damage response / dendrite / protein kinase binding / protein-containing complex binding / enzyme binding / DNA binding / extracellular region / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Microtubule-associated protein Tau / Microtubule associated protein, tubulin-binding repeat / Tau and MAP protein, tubulin-binding repeat / Tau and MAP proteins tubulin-binding repeat signature. / Tau and MAP proteins tubulin-binding repeat profile. / :
Similarity search - Domain/homology
Microtubule-associated protein tau
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsLovestam, S.L. / Scheres, S.H.W. / Goedert, M.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom) United Kingdom
CitationJournal: Nature / Year: 2026
Title: Prion-like transmission of human tau strains in the mouse brain.
Authors: Sofia Lövestam / Aki Shimozawa / Airi Tarutani / Reiko Ohtani / Masami Masuda-Suzukake / Kazuko Hasegawa / Andrew C Robinson / Yuko Saito / Shigeo Murayama / Mari Yoshida / Hisaomi Suzuki / ...Authors: Sofia Lövestam / Aki Shimozawa / Airi Tarutani / Reiko Ohtani / Masami Masuda-Suzukake / Kazuko Hasegawa / Andrew C Robinson / Yuko Saito / Shigeo Murayama / Mari Yoshida / Hisaomi Suzuki / Mitsumoto Onaya / Masato Hasegawa / Michel Goedert / Sjors H W Scheres /
Abstract: Most neurodegenerative diseases are thought to spread through the brain by prion-like mechanisms, in which filamentous protein assemblies self-propagate by templated seeding. Distinct conformations ...Most neurodegenerative diseases are thought to spread through the brain by prion-like mechanisms, in which filamentous protein assemblies self-propagate by templated seeding. Distinct conformations of amyloid filaments may provide the physical basis for the strains that lead to different diseases. However, a central pillar of the prion hypothesis, that strains retain their structural identity upon transmission, has not been demonstrated. Here we show that the injection of tau filaments from the brains of individuals with Alzheimer's disease or corticobasal degeneration into the brains of wild-type mice leads to the seeded assembly of amyloid filaments made of mouse tau with the same structures as those of the seeds. Thus, we show that, similar to prion strains, tau filaments propagate through templated seeding, and that the mouse is a suitable model to study the molecular mechanisms by which distinct tau folds drive disease-specific pathology in the brain.
History
DepositionMar 27, 2026Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 27, 2026Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.1Oct 14, 2026Group: Data collection / Database references / Category: citation / citation_author / em_admin
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Revision 1.1Oct 14, 2026Data content type: EM metadata / Data content type: EM metadata / EM metadata / Group: Database references / Experimental summary / Data content type: EM metadata / EM metadata / EM metadata / Category: citation / citation_author / em_admin
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Isoform Tau-A of Microtubule-associated protein tau
B: Isoform Tau-A of Microtubule-associated protein tau
C: Isoform Tau-A of Microtubule-associated protein tau
D: Isoform Tau-A of Microtubule-associated protein tau
E: Isoform Tau-A of Microtubule-associated protein tau
F: Isoform Tau-A of Microtubule-associated protein tau


Theoretical massNumber of molelcules
Total (without water)269,7716
Polymers269,7716
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
Isoform Tau-A of Microtubule-associated protein tau / Neurofibrillary tangle protein / Paired helical filament-tau / PHF-tau


Mass: 44961.766 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / References: UniProt: P10637
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: FILAMENT / 3D reconstruction method: helical reconstruction

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Sample preparation

ComponentName: Tau filament with the AD fold from mouse seeded by human AD tau seeds
Type: COMPLEX / Entity ID: all / Source: NATURAL
Source (natural)Organism: Mus (mice)
Buffer solutionpH: 7.2
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 40 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

EM software
IDNameVersionCategory
1RELION5.1particle selection
13RELION5.13D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: 179.446 ° / Axial rise/subunit: 2.42 Å / Axial symmetry: C1
3D reconstructionResolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 90623 / Symmetry type: HELICAL

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