2LFM: A Partially Folded Structure of Amyloid-beta(1 40) in an Aqueous Environment

Aggregation of the Abeta(1-40) peptide is linked to the development of extracellular plaques characteristic of Alzheimer's disease. While previous studies commonly show the Abeta(1-40) is largely unstructured in solution, we show that Abeta(1-40) can adopt a compact, partially folded structure. In this structure (PDB ID: 2LFM), the central hydrophobic region of the peptide forms a 3(10) helix from H13 to D23 and the N- and C-termini collapse against the helix due to the clustering of hydrophobic residues. Helical intermediates have been predicted to be crucial on-pathway intermediates in amyloid fibrillogenesis, and the structure presented here presents a new target for investigation of early events in Abeta(1-40) fibrillogenesis.
PDB ID: 2LFMDownload
MMDB ID: 92080
PDB Deposition Date: 2011/7/6
Updated in MMDB: 2011/08
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2LFM: monomeric; determined by author
Molecular Components in 2LFM
Label Count Molecule
Protein (1 molecule)
Beta-amyloid Protein 40(Gene symbol: APP)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB