› 2lnq

Solid-state NMR

40-residue D23N beta amyloid fibril

Released:
DOI: 10.2210/pdb2lnq/pdb
PDB entry 2lnq coloured by chain, ensemble of 10 models, front view.
PDB entry 2lnq coloured by chain, ensemble of 10 models, side view.
PDB entry 2lnq coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils.
Qiang W, Yau WM, Luo Y, Mattson MP, Tycko R
Proc Natl Acad Sci U S A 109 4443-8 (2012)
PMID: 22403062

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138403 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid-beta protein 40 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 40 amino acids
Theoretical weight: 4.33 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 672-711; Coverage: 5%)
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
Chemical shift assignment: 3%
Refinement method: simulated annealing
Expression system: Not provided

Quick links

Citations

37 review citations

A new era for understanding amyloid structures and disease.
Iadanza et al. (2018)
36 more

34 mentions without citation

Amyloid polymorphism: structural basis and neurobiological relevance.
Tycko R. (2015)
33 more