2LFM
A partially folded structure of amyloid-beta(1 40) in an aqueous environment
Summary for 2LFM
| Entry DOI | 10.2210/pdb2lfm/pdb |
| NMR Information | BMRB: 17764 |
| Descriptor | Beta-amyloid protein 40 (1 entity in total) |
| Functional Keywords | protein fibril |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Single-pass type I membrane protein: P05067 |
| Total number of polymer chains | 1 |
| Total formula weight | 4335.85 |
| Authors | Vivekanandan, S.,Brender, J.R.,Lee, S.Y.,Ramamoorthy, A. (deposition date: 2011-07-06, release date: 2011-07-20, Last modification date: 2024-05-15) |
| Primary citation | Vivekanandan, S.,Brender, J.R.,Lee, S.Y.,Ramamoorthy, A. A partially folded structure of amyloid-beta(1-40) in an aqueous environment. Biochem.Biophys.Res.Commun., 411:312-316, 2011 Cited by PubMed Abstract: Aggregation of the Aβ(1-40) peptide is linked to the development of extracellular plaques characteristic of Alzheimer's disease. While previous studies commonly show the Aβ(1-40) is largely unstructured in solution, we show that Aβ(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 Aβ(1-40) fibrillogenesis. PubMed: 21726530DOI: 10.1016/j.bbrc.2011.06.133 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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