› 2mxu

Solid-state NMR

42-Residue Beta Amyloid Fibril

Released:
DOI: 10.2210/pdb2mxu/pdb
PDB entry 2mxu coloured by chain, ensemble of 10 models, front view.
PDB entry 2mxu coloured by chain, ensemble of 10 models, side view.
PDB entry 2mxu coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease.
Xiao Y, Ma B, McElheny D, Parthasarathy S, Long F, Hoshi M, Nussinov R, Ishii Y
Nat Struct Mol Biol 22 499-505 (2015)
PMID: 25938662

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 42 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: 42 amino acids
Theoretical weight: 4.52 KDa
Source organism: Homo sapiens
Expression system: Not provided
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
Chemical shift assignment: 2%
Refinement method: torsion angle dynamics, simulated annealing
Expression system: Not provided

Quick links

Citations

62 review citations

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

85 mentions without citation

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.
Nguyen et al. (2021)
84 more