6OC9
S8 phosphorylated beta amyloid 40 fibrils
Summary for 6OC9
| Entry DOI | 10.2210/pdb6oc9/pdb |
| NMR Information | BMRB: 30596 |
| Descriptor | Amyloid-beta precursor protein, PHOSPHONATE (2 entities in total) |
| Functional Keywords | amyloid fibrils, beta amyloid, phosphorylation, post-translational modification, signaling protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 10 |
| Total formula weight | 44158.32 |
| Authors | |
| Primary citation | Hu, Z.W.,Vugmeyster, L.,Au, D.F.,Ostrovsky, D.,Sun, Y.,Qiang, W. Molecular structure of an N-terminal phosphorylated beta-amyloid fibril. Proc.Natl.Acad.Sci.USA, 116:11253-11258, 2019 Cited by PubMed Abstract: The structural polymorphism in β-amyloid (Aβ) plaques from Alzheimer disease (AD) has been recognized as an important pathological factor. Plaques from sporadic AD patients contain fibrillar deposits of various amyloid proteins/peptides, including posttranslational modified Aβ (PTM-Aβ) subtypes. Although many PTM-Aβs were shown to accelerate the fibrillation process, increase neuronal cytotoxicity of aggregates, or enhance the stability of fibrils, the contribution of PTM-Aβs to structural polymorphisms and their pathological roles remains unclear. We report here the NMR-based structure for the Ser-8-phosphorylated 40-residue Aβ (pS8-Aβ) fibrils, which shows significant difference to the wild-type fibrils, with higher cross-seeding efficiency and thermodynamic stability. Given these physicochemical properties, the structures originated from pS8-Aβ fibrils may potentially dominate the polymorphisms in the mixture of wild-type and phosphorylated Aβ deposits. Our results imply that Aβ subtypes with "seeding-prone" properties may influence the polymorphisms of amyloid plaques through the cross-seeding process. PubMed: 31097588DOI: 10.1073/pnas.1818530116 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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