› 2lmo

Solid-state NMR

Structural Model for a 40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry, Negative Stagger

Released:
DOI: 10.2210/pdb2lmo/pdb
PDB entry 2lmo coloured by chain, ensemble of 10 models, front view.
PDB entry 2lmo coloured by chain, ensemble of 10 models, side view.
PDB entry 2lmo coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils.
Paravastu AK, Leapman RD, Yau WM, Tycko R
Proc Natl Acad Sci U S A 105 18349-54 (2008)
PMID: 19015532

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138392 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid-beta protein 40 Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 40 amino acids
Theoretical weight: 4.34 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: 2%
Refinement method: simulated annealing
Expression system: Not provided

Quick links

Citations

115 review citations

Nanomechanics of functional and pathological amyloid materials.
Knowles et al. (2011)
114 more

43 mentions without citation

Molecular structures of amyloid and prion fibrils: consensus versus controversy.
Tycko et al. (2013)
42 more