› 2beg

Solution NMR

3D Structure of Alzheimer's Abeta(1-42) fibrils

Released:
DOI: 10.2210/pdb2beg/pdb
PDB entry 2beg coloured by chain, ensemble of 10 models, front view.
PDB entry 2beg coloured by chain, ensemble of 10 models, side view.
PDB entry 2beg coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
3D structure of Alzheimer's amyloid-beta(1-42) fibrils.
Lührs T, Ritter C, Adrian M, Riek-Loher D, Bohrmann B, Döbeli H, Schubert D, Riek R
Proc Natl Acad Sci U S A 102 17342-7 (2005)
PMID: 16293696

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138401 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid-beta protein 42 Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 42 amino acids
Theoretical weight: 4.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05067 (Residues: 672-713; Coverage: 6%)
Gene names: A4, AD1, APP
Sequence domains: Beta-amyloid peptide (beta-APP)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

163 review citations

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

192 mentions without citation

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