4CEG

Crystal structure of Aurora A 122-403 C290A, C393A bound to ADP

4CEG の概要

• エントリーDOI: 10.2210/pdb4ceg/pdb
• 分子名称: AURORA KINASE A, ADENOSINE-5'-DIPHOSPHATE, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: transferase, protein kinase, mitosis
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33766.45

構造登録者

Burgess, S.G.,Bayliss, R. (登録日: 2013-11-11, 公開日: 2015-01-28, 最終更新日: 2024-11-06)

主引用文献

Burgess, S.G.,Bayliss, R.
The Structure of C290A:C393A Aurora a Provides Structural Insights Into Kinase Regulation.
Acta Crystallogr.,Sect.F, 71:315-, 2015

PubMed Abstract: Aurora A is a Ser/Thr protein kinase that functions in cell-cycle regulation and is implicated in cancer development. During mitosis, Aurora A is activated by autophosphorylation on its activation loop at Thr288. The Aurora A catalytic domain (amino acids 122-403) expressed in Escherichia coli autophosphorylates on two activation-loop threonine residues (Thr288 and Thr287), whereas a C290A,C393A double point mutant of the Aurora A catalytic domain autophosphorylates only on Thr288. The structure of the complex of this mutant with ADP and magnesium was determined to 2.1 Å resolution using molecular replacement. This is an improvement on the existing 2.75 Å resolution structure of the equivalent wild-type complex. The structure confirms that single phosphorylation of the activation loop on Thr288 is insufficient to stabilize a `fully active' conformation of the activation loop in the absence of binding to TPX2.

PubMed: 25760707
DOI: 10.1107/S2053230X15002290

実験手法

X-RAY DIFFRACTION (2.1 Å)