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The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification 1
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)
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Metadata
- Authors
- Hanks, S. K., & Hunter, T.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 1995-05
- Volume
- 9
- Issue
- 8
- Pages
- 576-596
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W4295216797
- Cited by
- 2,318
- References
- 0
- FWCI
- 24.04
- Type
- journal article
- Language
- en
- Open access
- closed
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- Hanks, S. K., & Hunter, T. (1995). The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification 1. The FASEB Journal. https://doi.org/10.1096/fasebj.9.8.7768349
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