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Publication : Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.

First Author  Hanks SK Year  1995
Journal  FASEB J Volume  9
Issue  8 Pages  576-96
PubMed ID  7768349 Mgi Jnum  J:25921
Mgi Id  MGI:73624 Doi  10.1096/fasebj.9.8.7768349
Citation  Hanks SK, et al. (1995) Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J 9(8):576-96
abstractText  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.
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