S
IPR017441

Protein kinase, ATP binding site

InterPro entry
Short nameProtein_kinase_ATP_BS

Description

Eukaryotic protein kinases
[2, 3, 4, 5, 6]
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.

This entry represents a conserved site, which is located in the N-terminal extremity of the catalytic domain, where there is a glycine-rich stretch of residues in the vicinity of a lysine residue. It is this lysine residue that has been shown to be involved in ATP binding.

Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity
[6]
:


 * Serine/threonine-protein kinases
 * Tyrosine-protein kinases
 * Dual specificity protein kinases (e.g. MEK -phosphorylates both Thr and Tyr on target proteins)


Protein kinase function is evolutionarily conserved from Escherichia coli to human
[1]
. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation
[7]
. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved
[8]
, leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases
[9]
.

References

1.The protein kinase complement of the human genome. Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S. Science 298, 1912-34, (2002). View articlePMID: 12471243

2.Genomic analysis of the eukaryotic protein kinase superfamily: a perspective. Hanks SK. Genome Biol. 4, 111, (2003). View articlePMID: 12734000

3.Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. Hanks SK, Hunter T. FASEB J. 9, 576-96, (1995). View articlePMID: 7768349

4.Protein kinase classification. Hunter T. Meth. Enzymol. 200, 3-37, (1991). View articlePMID: 1835513

5.Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Hanks SK, Quinn AM. Meth. Enzymol. 200, 38-62, (1991). View articlePMID: 1956325

6.The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Hanks SK, Quinn AM, Hunter T. Science 241, 42-52, (1988). View articlePMID: 3291115

7.Evolution of protein kinase signaling from yeast to man. Manning G, Plowman GD, Hunter T, Sudarsanam S. Trends Biochem. Sci. 27, 514-20, (2002). View articlePMID: 12368087

8.High-throughput structural biology in drug discovery: protein kinases. Stout TJ, Foster PG, Matthews DJ. Curr. Pharm. Des. 10, 1069-82, (2004). View articlePMID: 15078142

9.Creating chemical diversity to target protein kinases. Li B, Liu Y, Uno T, Gray N. Comb. Chem. High Throughput Screen. 7, 453-72, (2004). View articlePMID: 15320712

GO terms

biological process

  • None

molecular function

cellular component

  • None

Cross References

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