Abstract
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 ≈ 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 severed 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, S. K., Hunter, T. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576‐596 (1995)
Keywords
Protein superfamilyBiochemistryc-RafKinaseProtein kinase domainMAP2K7SH3 domainBiologySerineProtein kinase AChemistryCyclin-dependent kinase 2EnzymeReceptor tyrosine kinaseGene
MeSH Terms
Amino Acid SequenceBinding SitesCatalysisEukaryotic CellsForecastingHumansMolecular Sequence DataProtein ConformationProtein KinasesSequence HomologyAmino Acid
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Publication Info
- Year
- 1995
- Type
- article
- Volume
- 9
- Issue
- 8
- Pages
- 576-596
- Citations
- 2278
- Access
- Closed
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Cite This
Steven K. Hanks,
Tony Hunter
(1995).
The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification <sup>1</sup>.
The FASEB Journal
, 9
(8)
, 576-596.
https://doi.org/10.1096/fasebj.9.8.7768349
Identifiers
- DOI
- 10.1096/fasebj.9.8.7768349
- PMID
- 7768349