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

TLDR

Eukaryotic protein kinases form a large superfamily defined by a ~250‑300 residue catalytic domain containing 12 conserved subdomains that fold into a common core, subdivided into serine/threonine and tyrosine kinases. The authors propose a classification scheme based on kinase domain phylogeny to group enzymes by substrate specificity and regulatory mode. They construct a phylogenetic tree of kinase domains to delineate families with shared substrate preferences and regulatory mechanisms.

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 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.