The structure of C290A:C393A Aurora A provides structural insights into kinase regulation

Acta Crystallographica. Section F, Structural Biology Communications
Selena G Burgess, Richard Bayliss

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.

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Citations

Apr 14, 2016·Theoretical Chemistry Accounts·Maria Grazia ConcilioSelena G Burgess
Jul 15, 2016·Open Biology·Selena G BurgessRichard Bayliss
Nov 12, 2016·Proceedings of the National Academy of Sciences of the United States of America·Mark W RichardsRichard Bayliss
Dec 27, 2016·Free Radical Biology & Medicine·Guang-Fei WangXuan Liu
Jul 3, 2015·PLoS Genetics·Selena G BurgessRichard Bayliss
Feb 13, 2019·Journal of Cellular Biochemistry·Garima Tanwar, Rituraj Purohit
Sep 29, 2019·Cellular and Molecular Life Sciences : CMLS·Giulia Bertolin, Marc Tramier
Jul 13, 2017·Angewandte Chemie·James A H GilburtCharlotte A Dodson
Dec 7, 2018·Proceedings of the National Academy of Sciences of the United States of America·Eric W LakeNicholas M Levinson
Jul 23, 2020·Science Signaling·Daniel C LimMichael B Yaffe
Jun 18, 2017·Biochemical Society Transactions·Richard BaylissMark W Richards

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