ArticleActa crystallographica. Section F, Structural biology communications2015
The structure of C290A:C393A Aurora A provides structural insights into kinase regulation.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 41 citations in OpenAlex.
- The ATC12 small molecule inhibits the Aurora-A/TPX2 interaction and impairs the proliferation of breast cancer cells.Cell death & disease · 2026Article
- Molecular basis for the activation of Aurora A and Plk1 kinases during mitotic entry.The EMBO journal · 2026Article
- The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A.Nature communications · 2026Article
- Bora bridges Aurora-A activation and substrate recognition of PLK1.EMBO reports · 2026Article
- Investigating the bioorthogonality of isocyanides.Chemical communications (Cambridge, England) · 2026Article
- Exploring the dynamics and interactions of the N-myc transactivation domain through solution nuclear magnetic resonance spectroscopy.The Biochemical journal · 2024Article
- CEP192 localises mitotic Aurora-A activity by priming its interaction with TPX2.The EMBO journal · 2024Article
- Inhibition of Aurora-A/N-Myc Protein-Protein Interaction Using Peptidomimetics: Understanding the Role of Peptide Cyclization.Chembiochem : a European journal of chemical biology · 2024Article
- Structural basis for CEP192-mediated regulation of centrosomal AURKA.Science advances · 2023Article
- Phosphorylation, Mg-ADP, and Inhibitors Differentially Shape the Conformational Dynamics of the A-Loop of Aurora-A.Biomolecules · 2021Article
- Insights into the non-mitotic functions of Aurora kinase A: more than just cell division.Cellular and molecular life sciences : CMLS · 2020Review
- Covalent Aurora A regulation by the metabolic integrator coenzyme A.Redox biology · 2020Article
- Quantitative conformational profiling of kinase inhibitors reveals origins of selectivity for Aurora kinase activation states.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mitotic spindle association of TACC3 requires Aurora-A-dependent stabilization of a cryptic α-helix.The EMBO journal · 2018Article
- A dynamic mechanism for allosteric activation of Aurora kinase A by activation loop phosphorylation.eLife · 2018Article
- Dynamic Equilibrium of the Aurora A Kinase Activation Loop Revealed by Single-Molecule Spectroscopy.Angewandte Chemie (International ed. in English) · 2017Article
- Structural basis of N-Myc binding by Aurora-A and its destabilization by kinase inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Allosteric inhibition of Aurora-A kinase by a synthetic vNAR domain.Open biology · 2016Article
- Non-centrosomal TPX2-Dependent Regulation of the Aurora A Kinase: Functional Implications for Healthy and Pathological Cell Division.Frontiers in oncology · 2016Review
- 7-(Pyrazol-4-yl)-3H-imidazo[4,5-b]pyridine-based derivatives for kinase inhibition: Co-crystallisation studies with Aurora-A reveal distinct differences in the orientation of the pyrazole N1-substituent.Bioorganic & medicinal chemistry letters · 2015Article
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2 authors at 1 institution in 1 country.
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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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