› 4np8

X-ray diffraction
1.51Å resolution

Structure of an amyloid forming peptide VQIVYK from the second repeat region of tau (alternate polymorph)

Released:
DOI: 10.2210/pdb4np8/pdb
PDB entry 4np8 coloured by chain, front view.
PDB entry 4np8 coloured by chain, side view.
PDB entry 4np8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular mechanisms for protein-encoded inheritance.
Wiltzius JJ, Landau M, Nelson R, Sawaya MR, Apostol MI, Goldschmidt L, Soriaga AB, Cascio D, Rajashankar K, Eisenberg D
Nat Struct Mol Biol 16 973-8 (2009)
PMID: 19684598

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145404 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Microtubule-associated protein tau Chain: A
Molecule details ›
Chain: A
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: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 28.635Å b: 4.88Å c: 35.807Å
α: 90° β: 110.47° γ: 90°
R-values:
R R work R free
0.179 0.177 0.196
Expression system: Not provided

Quick links

Citations

40 review citations

The amyloid state of proteins in human diseases.
Eisenberg et al. (2012)
39 more

5 mentions without citation

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