Techniques to examine nucleotide binding by pseudokinases

Isabelle Lucet, Jeffrey Babon, James M Murphy

Research output: Contribution to journalArticleResearchpeer-review

12 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)975 - 980
Number of pages6
JournalBiochemical Society Transactions
Volume41
Issue number4
DOIs
Publication statusPublished - 2013

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