› 4e0m

X-ray diffraction
1.75Å resolution

SVQIVYK segment from human Tau (305-311) displayed on 54-membered macrocycle scaffold (form I)

Released:
DOI: 10.2210/pdb4e0m/pdb
PDB entry 4e0m coloured by chain, front view.
PDB entry 4e0m coloured by chain, side view.
PDB entry 4e0m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates.
Liu C, Zhao M, Jiang L, Cheng PN, Park J, Sawaya MR, Pensalfini A, Gou D, Berk AJ, Glabe CG, Nowick J, Eisenberg D
Proc Natl Acad Sci U S A 109 20913-8 (2012)
PMID: 23213214

Function and Biology Details

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

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: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 14 amino acids
Theoretical weight: 1.93 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P10636 (Residues: 621-628; Coverage: 1%)
Gene names: MAPT, MAPTL, MTBT1, TAU

Ligands and Environments

2 bound ligands:
Ligand PO4 7 x PO4
Ligand MPD 2 x MPD
1 modified residue:
Ligand ORN 8 x ORN

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 58.32Å b: 25.34Å c: 50.78Å
α: 90° β: 122.19° γ: 90°
R-values:
R R work R free
0.189 0.185 0.221
Expression system: Not provided

Quick links

Citations

25 review citations

Self-propagation of pathogenic protein aggregates in neurodegenerative diseases.
Jucker et al. (2013)
24 more

4 mentions without citation

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