9F07

TUBULIN:STATHMIN:DARPIN:TAU MTBR3 COMPLEX

Summary for 9F07

• Entry DOI: 10.2210/pdb9f07/pdb
• Descriptor: Tubulin alpha chain, PENTAETHYLENE GLYCOL, HEXAETHYLENE GLYCOL, ... (13 entities in total)
• Functional Keywords: microtubule tau fusion protein, cell cycle
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 8
• Total formula weight: 270167.94

Authors

Ammar Khodja, L.,Campanacci, V.,Gigant, b. (deposition date: 2024-04-15, release date: 2024-11-13, Last modification date: 2024-11-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.211 Å)