Approximately 10% of the human kinome has been classified as pseudokinases due to the absence of one or more of three motifs known to play key roles in the catalytic activities of protein kinases. Structural and functional studies are now emerging, reclassifying this ‘dead’ kinase family as essential signalling molecules that act as crucial modulators of signal transduction. This raises the prospect that pseudokinases may well represent an as-yet-unexplored class of drug targets. However, the extent to which nucleotide binding and catalytic activity contribute to the biological functions of pseudokinases remains an area of great controversy. In the present review, we discuss the advantages and disadvantages of the different methods employed to characterize the nucleotide-binding properties and activity of pseudokinases.
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August 2013
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Conference Article|
July 18 2013
Techniques to examine nucleotide binding by pseudokinases
Isabelle S. Lucet;
Isabelle S. Lucet
1
*Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Wellington Road, Clayton, VIC 3800, Australia
1To whom correspondence should be addressed (emailIsabelle.lucet@monash.edu).
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Jeffrey J. Babon;
Jeffrey J. Babon
†Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, VIC 3052, Australia
‡Department of Medical Biology, University of Melbourne, 1G Royal Parade, Parkville, VIC 3052, Australia
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James M. Murphy
James M. Murphy
†Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, VIC 3052, Australia
‡Department of Medical Biology, University of Melbourne, 1G Royal Parade, Parkville, VIC 3052, Australia
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Publisher: Portland Press Ltd
Received:
May 03 2013
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2013 Biochemical Society
2013
Biochem Soc Trans (2013) 41 (4): 975–980.
Article history
Received:
May 03 2013
Citation
Isabelle S. Lucet, Jeffrey J. Babon, James M. Murphy; Techniques to examine nucleotide binding by pseudokinases. Biochem Soc Trans 1 August 2013; 41 (4): 975–980. doi: https://doi.org/10.1042/BST20130075
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