User:Alice Harmon/Sandbox 1: Difference between revisions

Line 1:

'''Eukaryotic Protein Kinase'''

'''Eukaryotic Protein Kinase Catalytic Domain'''

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, responses to the environment, and in diseases such as cancer.

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, responses to the environment, and in diseases such as cancer. Baker's yeast have ? protein kinase genes (?% of the genome),and humans and rice have ? (?%) and ? (?%), respectively.

~~In 1985~~ Hanks, Quinn, and Hunter ~~provided the first analysis of protein kinase structure,~~ based upon the alignment of amino acid sequences of 65 protein kinases~~. In 1995~~, ~~Taylor et al, published the first x-ray crystal structure of a protein kinase, which was protein kinase A (PKA). The crystal structure~~ and ~~extensive biochemical work on PKA established it as a model for all eukaryotic protein kinases. The pioneering analysis of the primary structure of protein kinases (~~revised by Hanks and Hunter in 1995) and the three dimensional structure of PKA ~~have proven~~ to ~~apply~~ to the great range of protein kinases known today. ~~Baker's yeast have ? protein kinase genes (?% of the genome),and humans and rice have ? (?%) and ? (?%), respectively.~~

This article is based on the pioneering analysis of the primary structure of protein kinases by Hanks, Quinn, and Hunter based upon the alignment of amino acid sequences of 65 protein kinases, and revised by Hanks and Hunter in 1995, and on the first three dimensional structure of protein kinase, that of PKA, to be published. The results described in these papers applies to the great range of protein kinases known today.

~~Here~~, the ~~twelve conserved subdomains defined by Hanks~~ and ~~Hunter are examined using PKA as~~ the ~~model~~ protein. The crystal structure includes ATP.2Mg2+ and the inhibitor peptide that has an alanine substituted for serine in a substrate's phosphorylation motif RRxS. All of the scenes below include ATP, and some include the inhibitor peptide to illustrate kinase/substrate interactions.

The catalytic domains of eukaryotic protein kinases have a small lobe and a large lobe (seen at the top and bottom of the model, respectively), and the catalytic site is located in a cleft between them. The small lobe binds ATP and the small lobe binds the protein substrate. The crystal structure includes ATP.2Mg2+ and the inhibitor peptide that has an alanine substituted for serine in a substrate's phosphorylation motif RRxS. All of the molecular scenes below include ATP, and some include the inhibitor peptide to illustrate kinase/substrate interactions.

Here, the twelve conserved subdomains defined by Hanks and Hunter are examined using PKA as the model protein.

<scene name='55/555705/Subdomaini/1'>Subdomain I</scene> contains two beta strands connected by the glycine rich ATP-binding loop with the motif <scene name='55/555705/Gxgxxg/1'>GxGxxG</scene> shown in ball and stick.

@@ Line 1: / Line 1: @@
-'''Eukaryotic Protein Kinase'''
+'''Eukaryotic Protein Kinase Catalytic Domain'''
-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, responses to the environment, and in diseases such as cancer.
+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, responses to the environment, and in diseases such as cancer.   Baker's yeast have ? protein kinase genes (?% of the genome),and humans and rice have ? (?%) and ? (?%), respectively.
-In 1985 Hanks, Quinn, and Hunter provided the first analysis of protein kinase structure, based upon the alignment of amino acid sequences of 65 protein kinases. In 1995, Taylor et al,  published the first x-ray crystal structure of a protein kinase, which was protein kinase A (PKA). The crystal structure and extensive biochemical work on PKA established it as a model for all eukaryotic protein kinases. The pioneering analysis of the primary structure of protein kinases (revised by Hanks and Hunter in 1995) and the three dimensional  structure of PKA have proven to apply to the great range of protein kinases known today. Baker's yeast have ? protein kinase genes (?% of the genome),and humans and rice have ? (?%) and ? (?%), respectively.
+This article is based on the pioneering analysis of the primary structure of protein kinases by Hanks, Quinn, and Hunter based upon the alignment of amino acid sequences of 65 protein kinases, and revised by Hanks and Hunter in 1995, and on the first three dimensional structure of protein kinase, that of PKA, to be published. The results described in these papers applies to the great range of protein kinases known today.
-Here, the twelve conserved subdomains defined by Hanks and Hunter are examined using PKA as the model protein. The crystal structure includes ATP.2Mg2+ and the inhibitor peptide that has an alanine substituted for serine in a substrate's phosphorylation motif RRxS. All of the scenes below include ATP, and some include the inhibitor peptide to illustrate kinase/substrate interactions.
+The catalytic domains of eukaryotic protein kinases have a small lobe and a large lobe (seen at the top and bottom of the model, respectively), and the catalytic site is located in a cleft between them. The small lobe binds ATP and the small lobe binds the protein substrate. The crystal structure includes ATP.2Mg2+ and the inhibitor peptide that has an alanine substituted for serine in a substrate's phosphorylation motif RRxS. All of the molecular scenes below include ATP, and some include the inhibitor peptide to illustrate kinase/substrate interactions.
-<Structure load='1ATP' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
+Here, the twelve conserved subdomains defined by Hanks and Hunter are examined using PKA as the model protein.
+<Structure load='1ATP' size='500' frame='true' align='right' caption='Protein kinase A in complex with ATP, magnesium and inhibitor peptide' scene='Insert optional scene name here' />
 <scene name='55/555705/Subdomaini/1'>Subdomain I</scene> contains two beta strands connected by the glycine rich ATP-binding loop with the motif <scene name='55/555705/Gxgxxg/1'>GxGxxG</scene> shown in ball and stick.