Techniques to examine nucleotide binding by pseudokinases
- Author(s)
- Lucet, IS; Babon, JJ; Murphy, JM;
- Journal Title
- BIOCHEMICAL SOCIETY TRANSACTIONS
- Publication Type
- Journal Article
- Abstract
- 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.
- Publisher
- PORTLAND PRESS LTD
- Research Division(s)
- Cancer And Haematology; Structural Biology
- PubMed ID
- 23863166
- Publisher's Version
- https://doi.org/10.1042/BST20130075
- NHMRC Grants
- NHMRC/361646, NHMRC/637342,
- Terms of Use/Rights Notice
- © The Authors Journal compilation © 2013 Biochemical Society
Creation Date: 2013-08-01 12:00:00
Last Modified: 2018-01-15 04:31:13