Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/31737
Title: The structure of C290A:C393A Aurora A provides structural insights into kinase regulation
Authors: Burgess, Selena G.
Bayliss, Richard
First Published: 2015
Publisher: International Union of Crystallography
Citation: Acta Crystallographica Section F: Structural Biology and Crystallization Communications Online
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.
DOI Link: 10.1107/S2053230X15002290
ISSN: 1744-3091
Links: http://scripts.iucr.org/cgi-bin/paper?S2053230X15002290
http://hdl.handle.net/2381/31737
Version: Post-print
Status: Peer-reviewed
Type: Journal Article
Rights: Archived with reference to SHERPA/RoMEO and publisher website.
Description: PDB reference: 4ceg http://www.rcsb.org/pdb/explore.do?structureId=4ceg
Appears in Collections:Published Articles, Dept. of Biochemistry

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