› 6vi3

Electron Microscopy
3.3Å resolution

Straight Filament from Alzheimer's Disease Human Brain Tissue

Released:
DOI: 10.2210/pdb6vi3/pdb
PDB entry 6vi3 coloured by chain, front view.
PDB entry 6vi3 coloured by chain, side view.
PDB entry 6vi3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Posttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains.
Arakhamia T, Lee CE, Carlomagno Y, Duong DM, Kundinger SR, Wang K, Williams D, DeTure M, Dickson DW, Cook CN, Seyfried NT, Petrucelli L, Fitzpatrick AWP
Cell 180 633-644.e12 (2020)
PMID: 32032505
Related structures: EMD-0260

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145398 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Microtubule-associated protein tau Chains: E, F
Molecule details ›
Chains: E, F
Length: 77 amino acids
Theoretical weight: 8.37 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P10636 (Residues: 621-697; Coverage: 10%)
Gene names: MAPT, MAPTL, MTBT1, TAU
Sequence domains: Tau and MAP protein, tubulin-binding repeat

Ligands and Environments

1 bound ligand:
Ligand GLY 2 x GLY
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.3Å
Relevant EMDB volumes: EMD-0260
Expression system: Homo sapiens

Quick links

Citations

69 review citations

Protein transmission in neurodegenerative disease.
Peng et al. (2020)
68 more

3 mentions without citation

Insights into the Structural Conformations of the Tau Protein in Different Aggregation Status.
Pinzi et al. (2023)
2 more