Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.
The eukaryotic protein kinases make up a large superfamily of homologous proteins. They are related by virtue of their kinase domains (also known as catalytic domains), which consist of approximately 250-300 amino acid residues. The kinase domains that define this group of enzymes contain 12 conserved subdomains that fold into a common catalytic core structure, as revealed by the 3-dimensional structures of several protein-serine kinases. There are two main subdivisions within the superfamily: the protein-serine/threonine kinases and the protein-tyrosine kinases. A classification scheme can be founded on a kinase domain phylogeny, which reveals families of enzymes that have related substrate specificities and modes of regulation.
Hanks
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Department of Cell Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA.
Hunter
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D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D005057:Eukaryotic Cells / Q000201:enzymology*; D005544:Forecasting; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry* / Q000145:classification*; D017386:Sequence Homology, Amino Acid
D011494:Protein Kinases