3E22

Tubulin-colchicine-soblidotin: Stathmin-like domain complex

3E22 の概要

• エントリーDOI: 10.2210/pdb3e22/pdb
• 関連するPDBエントリー: 1SA0 1Z2B 3DU7
• 分子名称: Tubulin alpha-1C chain, Tubulin beta-2B chain, Stathmin-4, ... (8 entities in total)
• 機能のキーワード: alpha-tubulin, beta-tubulin, colchicine, gtpase, microtubule, soblidotin, stathmin, tubulin, cell cycle
• 由来する生物種: RATTUS NORVEGICUS (rat); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton (By similarity): Q3ZCJ7 Q6B856
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 220311.31

構造登録者

Cormier, A.,Marchand, M.,Ravelli, R.B.,Knossow, M.,Gigant, B. (登録日: 2008-08-05, 公開日: 2008-10-21, 最終更新日: 2023-11-01)

主引用文献

Cormier, A.,Marchand, M.,Ravelli, R.B.,Knossow, M.,Gigant, B.
Structural insight into the inhibition of tubulin by vinca domain peptide ligands
Embo Rep., 9:1101-1106, 2008

PubMed Abstract: The tubulin vinca domain is the target of widely different microtubule inhibitors that interfere with the binding of vinblastine. Although all these ligands inhibit the hydrolysis of GTP, they affect nucleotide exchange to variable extents. The structures of two vinca domain antimitotic peptides--phomopsin A and soblidotin (a dolastatin 10 analogue)--bound to tubulin in a complex with a stathmin-like domain show that their sites partly overlap with that of vinblastine and extend the definition of the vinca domain. The structural data, together with the biochemical results from the ligands we studied, highlight two main contributors in nucleotide exchange: the flexibility of the tubulin subunits' arrangement at their interfaces and the residues in the carboxy-terminal part of the beta-tubulin H6-H7 loop. The structures also highlight common features of the mechanisms by which vinca domain ligands favour curved tubulin assemblies and destabilize microtubules.

PubMed: 18787557
DOI: 10.1038/embor.2008.171

実験手法

X-RAY DIFFRACTION (3.8 Å)