› 5how

X-ray diffraction
2.3Å resolution

X-ray crystallographic structure of an Abeta 17-36 beta-hairpin. LV(PHI)FAEDCGSNKCAII(SAR)L(ORN)V

Released:
DOI: 10.2210/pdb5how/pdb
PDB entry 5how coloured by chain, front view.
PDB entry 5how coloured by chain, side view.
PDB entry 5how coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17-36 β-Hairpin.
Kreutzer AG, Hamza IL, Spencer RK, Nowick JS
J Am Chem Soc 138 4634-42 (2016)
PMID: 26967810

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dodecamer
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-138398 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
P3(40) Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 21 amino acids
Theoretical weight: 2.37 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 688-707; Coverage: 3%)
Gene names: A4, AD1, APP
Sequence domains: Beta-amyloid peptide (beta-APP)

Ligands and Environments

No bound ligands
3 modified residues:
Ligand ORN 12 x ORN
Ligand PHI 6 x PHI
Ligand SAR 6 x SAR

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P6122
Unit cell:
a: 97.31Å b: 97.31Å c: 97.621Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.236 0.234 0.262
Expression system: Not provided

Quick links

Citations

7 review citations

Structural studies of amyloid-β peptides: Unlocking the mechanism of aggregation and the associated toxicity.
Aleksis et al. (2017)
6 more

3 mentions without citation

Amyloid beta: structure, biology and structure-based therapeutic development.
Chen et al. (2017)
2 more