User:Alice Harmon/Sandbox 1: Difference between revisions

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==Eukaryotic Protein Kinase Catalytic Domain==

[[Image:1ATP.jpg|left|size='~~100~~']]

[[Image:1ATP.jpg|left|size='90']]

Eukaryotic protein kinases are enzymes that transfer a phosphoryl group (-PO32-) from adenosine triphosphate (or more rarely from adenosine diphosphate) to the hydroxyl group of serine, threonine, or tyrosine residue of a protein substrate. Phosphorylation of the substrate can affect its activity and/or conformation and, in turn, the physiogy of the cell. Protein kinases act as switches that turn on or off metabolic and signaling pathways, and they play central roles in development and responses to the environment. Also, unregulated versions of kinases that arise from tumor-promoting viruses promote cancer in humans. The number of protein kinase genes (and the percentage of the genome) in bakers yeast<ref>PMID: 9020587</ref>, humans<ref> PMID:12471243</ref> and rice<ref>PMID:17172291</ref> are 113 (2%),518 (2%), and 1429 (5%), respectively. The catalytic domains of these enzymes occur alone or with other functional domains in a single polypetide chain. Protein kinases may be monomeric or multimeric or found in complexes with regulatory proteins.

Eukaryotic protein kinases are enzymes that transfer a phosphoryl group (-PO32-) from adenosine triphosphate (or more rarely from adenosine diphosphate) to the hydroxyl group of serine, threonine, or tyrosine residue of a protein substrate. Phosphorylation of the substrate can affect its activity and/or conformation and, in turn, the physiogy of the cell. Protein kinases act as switches that turn on or off metabolic and signaling pathways, and they play central roles in development and responses to the environment. Also, unregulated versions of kinases that arise from tumor-promoting viruses promote cancer in humans. The number of protein kinase genes (and the percentage of the genome) in bakers yeast<ref>PMID: 9020587</ref>, humans<ref> PMID:12471243</ref> and rice<ref>PMID:17172291</ref> are 113 (2%), 518 (2%), and 1429 (5%), respectively. The catalytic domains of these enzymes occur alone or with other functional domains in a single polypetide chain. Protein kinases may be monomeric or multimeric or found in complexes with regulatory proteins.

This first section of this article relates the twelve conserved subdomains recognized in the primary structures of protein kinase catalytic domains<ref name='Hanksa'>PMID:3291115</ref><ref name='Hanksb'>PMID: 7768349</ref> to the three-dimensional structure of protein kinase A (also called PKA or [[CAMP-dependent protein kinase]])<ref name = 'Knightona'> PMID:1862342</ref><ref name = 'Knightonb'>PMID: 1862343</ref>. The results described in these classic papers apply to the basic structure of the great range of eukaryotic protein kinases known today.

The second section of this article examines functional structures and assemblies of protein kinase catalytic domains and compares active and inactive conformations.

==Tour of Structural Features==

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 ==Eukaryotic Protein Kinase Catalytic Domain==
-[[Image:1ATP.jpg|left|size='100']]
+[[Image:1ATP.jpg|left|size='90']]
-Eukaryotic protein kinases are enzymes that transfer a phosphoryl group (-PO<sub>3</sub><sup>2-</sup>) from adenosine triphosphate (or more rarely from adenosine diphosphate) to the hydroxyl group of serine, threonine, or tyrosine residue of a protein substrate. Phosphorylation of the substrate can affect its activity and/or conformation and, in turn, the physiogy of the cell. Protein kinases act as switches that turn on or off metabolic and signaling pathways, and they play central roles in development and responses to the environment. Also, unregulated versions of kinases that arise from tumor-promoting viruses promote cancer in humans.   The number of protein kinase genes (and the percentage of the genome) in bakers yeast<ref>PMID: 9020587</ref>, humans<ref> PMID:12471243</ref> and rice<ref>PMID:17172291</ref> are 113 (2%),518 (2%), and 1429 (5%), respectively. The catalytic domains of these enzymes occur alone or with other functional domains in a single polypetide chain. Protein kinases may be monomeric or multimeric or found in complexes with regulatory proteins.
+Eukaryotic protein kinases are enzymes that transfer a phosphoryl group (-PO<sub>3</sub><sup>2-</sup>) from adenosine triphosphate (or more rarely from adenosine diphosphate) to the hydroxyl group of serine, threonine, or tyrosine residue of a protein substrate. Phosphorylation of the substrate can affect its activity and/or conformation and, in turn, the physiogy of the cell. Protein kinases act as switches that turn on or off metabolic and signaling pathways, and they play central roles in development and responses to the environment. Also, unregulated versions of kinases that arise from tumor-promoting viruses promote cancer in humans.   The number of protein kinase genes (and the percentage of the genome) in bakers yeast<ref>PMID: 9020587</ref>, humans<ref> PMID:12471243</ref> and rice<ref>PMID:17172291</ref> are 113 (2%), 518 (2%), and 1429 (5%), respectively. The catalytic domains of these enzymes occur alone or with other functional domains in a single polypetide chain. Protein kinases may be monomeric or multimeric or found in complexes with regulatory proteins.
 This first section of this article relates the twelve conserved subdomains recognized in the primary structures of protein kinase catalytic domains<ref name='Hanksa'>PMID:3291115</ref><ref name='Hanksb'>PMID: 7768349</ref> to the three-dimensional structure of protein kinase A (also called PKA or [[CAMP-dependent protein kinase]])<ref name = 'Knightona'> PMID:1862342</ref><ref name = 'Knightonb'>PMID: 1862343</ref>. The results described in these classic papers apply to the basic structure of the great range of eukaryotic protein kinases known today.
 The second section of this article examines functional structures and assemblies of protein kinase catalytic domains and compares active and inactive conformations.
 ==Tour of Structural Features==