title: Techniques to examine nucleotide binding by pseudokinases.
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.
authors.affiliation: Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Wellington Road, Clayton, VIC 3800, Australia. Isabelle.lucet@monash.edu
authors.forename: Isabelle S
authors.initials: IS
authors.lastname: Lucet
authors.forename: Jeffrey J
authors.initials: JJ
authors.lastname: Babon
authors.forename: James M
authors.initials: JM
authors.lastname: Murphy
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D055162:Biocatalysis; D002846:Chromatography, Affinity; D018360:Crystallography, X-Ray; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D009711:Nucleotides / Q000378:metabolism*; D011485:Protein Binding; D011494:Protein Kinases / Q000378:metabolism*
chemical_list: D009711:Nucleotides; D000255:Adenosine Triphosphate; D011494:Protein Kinases