3UT5

Tubulin-Colchicine-Ustiloxin: Stathmin-like domain complex

3UT5 の概要

• エントリーDOI: 10.2210/pdb3ut5/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000814
• 分子名称: Tubulin alpha chain, Tubulin beta chain, Stathmin-4, ... (10 entities in total)
• 機能のキーワード: microtubules, tubulin, vinca domain, ustiloxin, stathmin, structural protein, structural protein-inhibitor complex, structural protein/inhibitor
• 由来する生物種: Rattus norvegicus (rat); 詳細
• 細胞内の位置: Golgi apparatus: P63043
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 220989.69

構造登録者

Ranaivoson, F.M.,Gigant, B.,Knossow, M. (登録日: 2011-11-25, 公開日: 2012-08-01, 最終更新日: 2024-11-06)

主引用文献

Ranaivoson, F.M.,Gigant, B.,Berritt, S.,Joullie, M.,Knossow, M.
Structural plasticity of tubulin assembly probed by vinca-domain ligands.
Acta Crystallogr.,Sect.D, 68:927-934, 2012

PubMed Abstract: Vinca-domain ligands are compounds that bind to tubulin at its inter-heterodimeric interface and favour heterogeneous protofilament-like assemblies, giving rise to helices and rings. This is the basis for their inhibition of microtubule assembly, for their antimitotic activities and for their use in anticancer chemotherapy. Ustiloxins are vinca-domain ligands with a well established total synthesis. A 2.7 Å resolution structure of ustiloxin D bound to the vinca domain embedded in the complex of two tubulins with the stathmin-like domain of RB3 (T(2)R) has been determined. This finding precisely defines the interactions of ustiloxins with tubulin and, taken together with structures of other vinca-ligand complexes, allows structure-based suggestions to be made for improved activity. These comparisons also provide a rationale for the large-scale polymorphism of the protofilament-like assemblies mediated by vinca-domain ligands based on local differences in their interactions with the two tubulin heterodimers constituting their binding site.

PubMed: 22868758
DOI: 10.1107/S0907444912017143

実験手法

X-RAY DIFFRACTION (2.73 Å)