6CVN

Model of synthetic tau (R2x4) bound to the microtubule

6CVN の概要

• エントリーDOI: 10.2210/pdb6cvn/pdb
• 関連するPDBエントリー: 6CVJ
• EMDBエントリー: 7522 7769 7771
• 分子名称: Tubulin beta chain, Tubulin alpha-1B chain, Microtubule-associated protein tau, ... (6 entities in total)
• 機能のキーワード: microtubule, tau, structural protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 172988.78

構造登録者

Nogales, E.,Kellogg, E.H. (登録日: 2018-03-28, 公開日: 2018-05-23, 最終更新日: 2024-03-13)

主引用文献

Kellogg, E.H.,Hejab, N.M.A.,Poepsel, S.,Downing, K.H.,DiMaio, F.,Nogales, E.
Near-atomic model of microtubule-tau interactions.
Science, 360:1242-1246, 2018

PubMed Abstract: Tau is a developmentally regulated axonal protein that stabilizes and bundles microtubules (MTs). Its hyperphosphorylation is thought to cause detachment from MTs and subsequent aggregation into fibrils implicated in Alzheimer's disease. It is unclear which tau residues are crucial for tau-MT interactions, where tau binds on MTs, and how it stabilizes them. We used cryo-electron microscopy to visualize different tau constructs on MTs and computational approaches to generate atomic models of tau-tubulin interactions. The conserved tubulin-binding repeats within tau adopt similar extended structures along the crest of the protofilament, stabilizing the interface between tubulin dimers. Our structures explain the effect of phosphorylation on MT affinity and lead to a model of tau repeats binding in tandem along protofilaments, tethering together tubulin dimers and stabilizing polymerization interfaces.

PubMed: 29748322
DOI: 10.1126/science.aat1780

実験手法

ELECTRON MICROSCOPY (3.9 Å)