12GB
High Resolution Structure of Monomorphic AB1-40 Fibrils
This is a non-PDB format compatible entry.
Summary for 12GB
| Entry DOI | 10.2210/pdb12gb/pdb |
| NMR Information | BMRB: 31300 |
| Descriptor | Type IIIb beta-amyloid 40 Filament (1 entity in total) |
| Functional Keywords | amyloid-beta, protein fibril, parallel in-register, cross-beta |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 20 |
| Total formula weight | 86717.04 |
| Authors | Bahri, S.,Palani, R.S.,Silvers, R.,Michael, B.,Lattanzi, V.,Andre, I.,Linse, S.,Griffin, R.G. (deposition date: 2026-04-03, release date: 2026-04-15, Last modification date: 2026-07-22) |
| Primary citation | Bahri, S.,Palani, R.S.,Silvers, R.,Michael, B.,Lattanzi, V.,Andre, I.,Linse, S.,Griffin, R.G. High-resolution structure of monomorphic A beta 1-40 fibrils. Proc.Natl.Acad.Sci.USA, 123:e2603575123-e2603575123, 2026 Cited by PubMed Abstract: Amyloid-β (Aβ) fibrils primarily composed of Aβ and Aβ form the core of senile plaques in Alzheimer's disease. Aβ fibrils may exhibit significant polymorphism influenced by sample preparation conditions, complicating atomic resolution structural characterization. To establish a reliable structural baseline, we developed a protocol for expressing and purifying recombinant Aβ that forms monomorphic fibrils under physiological conditions (pH 7.4). We present a high-resolution structure of these unseeded, monomorphic Aβ fibrils obtained using magic-angle spinning NMR spectroscopy (PDB ID 12GB). We obtained unambiguous chemical shift assignments for approximately 90% of the residues and measured over 500 distance and torsion angle restraints. The resolved structure, with a backbone RMSD of 0.63 ± 0.06 Å, shows two monomers per filament plane, with two distinct β-sheets (residues E11-E22 and K28-V39, respectively) running along the fibril axis with H-bonding between each plane, and the two strands linked by a flexible loop region. This structure reveals three continuous hydrophobic cores inside each filament which bury 24 hydrophobic side chains per filament plane: those of L17, F19, A21, V24, A30, I32, M35, V40 between the two β-strands within each monomer and I31, L34, V36, V39 between the two monomers. Small angle X-ray scattering reveals the size and geometry of the fibril cross-section, which is compatible with a two-filament arrangement with a total of 4 monomers per fibril plane. PubMed: 42418485DOI: 10.1073/pnas.2603575123 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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