Structure
The catalytic subunits of protein kinases are highly conserved, and several structures have been solved, leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases.
Eukaryotic protein kinases are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residue which is important for the catalytic activity of the enzyme.
Read more about this topic: Protein Kinase Domain
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“There is no such thing as a language, not if a language is anything like what many philosophers and linguists have supposed. There is therefore no such thing to be learned, mastered, or born with. We must give up the idea of a clearly defined shared structure which language-users acquire and then apply to cases.”
—Donald Davidson (b. 1917)