9F07

TUBULIN:STATHMIN:DARPIN:TAU MTBR3 COMPLEX

9F07 の概要

• エントリーDOI: 10.2210/pdb9f07/pdb
• 分子名称: Tubulin alpha chain, PENTAETHYLENE GLYCOL, HEXAETHYLENE GLYCOL, ... (13 entities in total)
• 機能のキーワード: microtubule tau fusion protein, cell cycle
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 270167.94

構造登録者

Ammar Khodja, L.,Campanacci, V.,Gigant, b. (登録日: 2024-04-15, 公開日: 2024-11-13, 最終更新日: 2024-11-27)

主引用文献

Ammar Khodja, L.,Campanacci, V.,Lippens, G.,Gigant, B.
The structure of a Tau fragment bound to tubulin prompts new hypotheses on Tau mechanism and oligomerization.
Pnas Nexus, 3:pgae487-pgae487, 2024

PubMed Abstract: Tau is a protein involved in the regulation of axonal microtubules in neurons. In pathological conditions, it forms filamentous aggregates which are molecular markers of neurodegenerative diseases known as tauopathies. Structures of Tau in fibrils or bound to the microtubule have been reported. We present here a structure of a Tau construct comprising the PHF6 motif, an oligopeptide involved in Tau aggregation, as a complex with tubulin. This Tau fragment binds as a dimer to a new site which, when transposed to the microtubule, would correspond to a pore between protofilaments. These results raise new hypotheses on Tau-induced microtubule assembly and stabilization and on Tau oligomerization.

PubMed: 39534653
DOI: 10.1093/pnasnexus/pgae487

実験手法

X-RAY DIFFRACTION (2.211 Å)