8G55
Temperature-dependent structures of tau aggregates
8G55 の概要
| エントリーDOI | 10.2210/pdb8g55/pdb |
| 関連するPDBエントリー | 8G54 |
| NMR情報 | BMRB: 31075 |
| 分子名称 | Microtubule-associated protein tau (1 entity in total) |
| 機能のキーワード | tau, amyloid fibril, protein fibril |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 10 |
| 化学式量合計 | 214516.41 |
| 構造登録者 | |
| 主引用文献 | El Mammeri, N.,Duan, P.,Dregni, A.J.,Hong, M. Amyloid fibril structures of tau: Conformational plasticity of the second microtubule-binding repeat. Sci Adv, 9:eadh4731-eadh4731, 2023 Cited by PubMed Abstract: The intrinsically disordered protein tau associates with microtubules in neurons but aggregates into cross-β amyloid fibrils that propagate in neurodegenerative brains. Different tauopathies have different structures for the rigid fibril core. To understand the molecular basis of tau assembly into different polymorphs, here we use solid-state nuclear magnetic resonance (NMR) spectroscopy to determine the structure of a tau protein that includes all microtubule-binding repeats and a proline-rich domain. This P2R tau assembles into well-ordered filaments when induced by heparin. Two- and three-dimensional NMR spectra indicate that R2 and R3 repeats constitute the rigid β-sheet core of the fibril. Unexpectedly, the amino-terminal half of R2 forms a β-arch at ambient temperature (24°C) but a continuous β-strand at 12°C, which dimerizes with the R2 of another protofilament. This temperature-dependent structure indicates that R2 is conformationally more plastic than the R3 domain. The distinct conformational stabilities of different microtubule-binding repeats give insight into the energy landscape of tau fibril formation. PubMed: 37450599DOI: 10.1126/sciadv.adh4731 主引用文献が同じPDBエントリー |
| 実験手法 | SOLID-STATE NMR |
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