1OL7

Structure of Human Aurora-A 122-403 phosphorylated on Thr287, Thr288

1OL7 の概要

• エントリーDOI: 10.2210/pdb1ol7/pdb
• 関連するPDBエントリー: 1MUO 1OL5 1OL6
• 分子名称: SERINE/THREONINE KINASE 6, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: kinase, cell cycle, transferase, serine/threonine-protein kinase, atp-binding, phosphorylation
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm, cytoskeleton, centrosome: O14965
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33325.23

構造登録者

Bayliss, R.,Conti, E. (登録日: 2003-08-06, 公開日: 2003-10-30, 最終更新日: 2024-11-20)

主引用文献

Bayliss, R.,Sardon, T.,Vernos, I.,Conti, E.
Structural Basis of Aurora-A Activation by Tpx2 at the Mitotic Spindle
Mol.Cell, 12:851-, 2003

PubMed Abstract: Aurora-A is an oncogenic kinase essential for mitotic spindle assembly. It is activated by phosphorylation and by the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. We have uncovered the molecular mechanism of Aurora-A activation by determining crystal structures of its phosphorylated form both with and without a 43 residue long domain of TPX2 that we identified as fully functional for kinase activation and protection from dephosphorylation. In the absence of TPX2, the Aurora-A activation segment is in an inactive conformation, with the crucial phosphothreonine exposed and accessible for deactivation. Binding of TPX2 triggers no global conformational changes in the kinase but pulls on the activation segment, swinging the phosphothreonine into a buried position and locking the active conformation. The recognition between Aurora-A and TPX2 resembles that between the cAPK catalytic core and its flanking regions, suggesting this molecular mechanism may be a recurring theme in kinase regulation.

PubMed: 14580337
DOI: 10.1016/S1097-2765(03)00392-7

実験手法

X-RAY DIFFRACTION (2.75 Å)