› 2on9

X-ray diffraction
1.51Å resolution

Structure of an amyloid forming peptide VQIVYK from the repeat region of Tau

Released:
DOI: 10.2210/pdb2on9/pdb
PDB entry 2on9 coloured by chain, front view.
PDB entry 2on9 coloured by chain, side view.
PDB entry 2on9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Atomic structures of amyloid cross-beta spines reveal varied steric zippers.
Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, Thompson MJ, Balbirnie M, Wiltzius JJ, McFarlane HT, Madsen AØ, Riekel C, Eisenberg D
Nature 447 453-7 (2007)
PMID: 17468747

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145401 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Microtubule-associated protein tau Chains: A, B
Molecule details ›
Chains: A, B
Length: 6 amino acids
Theoretical weight: 750 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P10636 (Residues: 623-628; Coverage: 1%)
Gene names: MAPT, MAPTL, MTBT1, TAU

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID13
Spacegroup: P21
Unit cell:
a: 4.863Å b: 61.926Å c: 15.413Å
α: 90° β: 98.11° γ: 90°
R-values:
R R work R free
0.207 0.206 0.225
Expression system: Not provided

Quick links

Citations

271 review citations

The amyloid state and its association with protein misfolding diseases.
Knowles et al. (2014)
270 more

30 mentions without citation

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