Structural Basis for Substrate Recognition and Control in Protein Kinases

  • L. N. Johnson
Conference paper
Part of the Ernst Schering Research Foundation Workshop book series (SCHERING FOUND, volume 34)


Protein kinases play key roles in eukaryotic signal transduction pathways (Hunter 2000). Phosphorylation of target proteins on serine, threonine, or tyrosine residues results in a number of different responses that include activation of enzyme activity, inhibition of enzyme activity, protein/protein recognition and association, protein/protein dissociation, and sub-cellular targeting. Consistent with their key roles in cellular signalling processes, the genome sequencing projects have revealed an approximate correlation in numbers of kinases and complexity of the organism. The genome of Escherichia coli contains no genuine eukaryotic protein kinase among its 4,288 genes, although it does contain several histidine kinases as part of the prokaryotic dual response mechanism to environmental factors. The genome of Mycobacterium tuberculosis, a bacterium that exhibits a more complex life style than E. coli, contains 11 protein kinase genes.


Peptide Substrate Substrate Recognition Phosphorylatable Serine Activation Segment Protein Kinase Gene 
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© Springer-Verlag Berlin Heidelberg 2001

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  • L. N. Johnson

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