Proteopedia - User contributions [en]

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-10T14:08:34Z

Andrew Menke:

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref> The N-terminus of the catalytic subunit is myristylated, although this is not shown in the electron density of this crystal structure. The myristylation does not confer membrane localization but stabilizes the enzyme to denaturation by a factor of 5. <ref>PMID: 8428909</ref>

==Activation and Interaction with Regulatory Subunit==
In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

==Binding to ATP==
Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits. The loop region that these occur in is referred to as the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'>glycine-rich loop</scene>. Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. The structural motif that the glycine rich loop is located in is a beta-strand, turn, beta-strand motif. These residues are also reported to have some role in phosphoryl transfer. <ref>PMID: 9202006</ref>

==Interaction with Substrate==
The larger C-terminal lobe of the kinase is responsible for substrate recognition. Several of the c-term lobes alpha helices are important in determining substrate recognition. The substrate mimic inhibitor <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Pki/1'>PKI</scene> demonstrates this nicely. The PKI inhibitor is a heat shock protein. It sits firmly within the catalytic cleft of the enzyme. <ref>PMID: 8443157</ref>

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-10T14:07:45Z

Andrew Menke:

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref> The N-terminus of the catalytic subunit is myristylated, although this is not shown in the electron density of this crystal structure. The myristylation does not confer membrane localization but stabilizes the enzyme to denaturation by a factor of 5. <ref>PMID: 8428909</ref>

==Activation and Interaction with Regulatory Subunit==
In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

==Binding to ATP==
Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits. The loop region that these occur in is referred to as the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'>glycine-rich loop</scene>. Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. The structural motif that the glycine rich loop is located in is a beta-strand, turn, beta-strand motif. These residues are also reported to have some role in phosphoryl transfer. <ref>PMID: 9202006</ref>

==Interaction with Substrate==
The larger C-terminal lobe of the kinase is responsible for substrate recognition. Several of the c-term lobes alpha helices are important in determining substrate recognition. The substrate mimic inhibitor <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Pki/1'>PKI</scene> demonstrates this nicely. The PKI inhibitor is a heat shock protein. It sits firmly within the catalytic cleft of the enzyme.
<ref>PMID: 8443157</ref>
==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-10T14:05:46Z

Andrew Menke:

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref> The N-terminus of the catalytic subunit is myristylated, although this is not shown in the electron density of this crystal structure. The myristylation does not confer membrane localization but stabilizes the enzyme to denaturation by a factor of 5. <ref>PMID: 8428909</ref>

==Activation and Interaction with Regulatory Subunit==
In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

==Binding to ATP==
Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits. The loop region that these occur in is referred to as the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'>glycine-rich loop</scene>. Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. The structural motif that the glycine rich loop is located in is a beta-strand, turn, beta-strand motif. These residues are also reported to have some role in phosphoryl transfer. <ref>PMID: 9202006</ref>

==Interaction with Substrate==
The larger C-terminal lobe of the kinase is responsible for substrate recognition. The substrate mimic inhibitor<scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Pki/1'>PKI</scene> demonstrates this nicely. <ref>PMID: 8443157</ref>

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-10T13:46:57Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T22:58:19Z

Andrew Menke:

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref> The N-terminus of the catalytic subunit is myristylated, although this is not shown in the electron density of this crystal structure. The myristylation does not confer membrane localization but stabilizes the enzyme to denaturation by a factor of 5. <ref>PMID: 8428909</ref>

==Activation and Interaction with Regulatory Subunit==
In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

==Binding to ATP==
Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits. The lopp region that these occur in is referred to as the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'>glycine-rich loop</scene>. Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. <ref>PMID: 9202006</ref>

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T22:11:48Z

Andrew Menke:

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref> The N-terminus of the catalytic subunit is myristylated, although this is not shown in the electron density of this crystal structure. The myristylation does not confer membrane localization but stabilizes the enzyme to denaturation by a factor of 5. <ref>PMID: 8428909</ref>

==Activation and Interaction with Regulatory Subunit==
[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

==Binding to ATP==
Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits. The lopp region that these occur in is referred to as the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'>glycine-rich loop</scene>. Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. <ref>PMID: 9202006</ref>

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T22:11:02Z

Andrew Menke:

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref> The N-terminus of the catalytic subunit is myristylated, although this is not shown in the electron density of this crystal structure. The myristylation does not confer membrane localization but stabilizes the enzyme to denaturation by a factor of 5. <ref>PMID: 8428909</ref>

==Activation and Interaction with Regulatory Subunit==
[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

<Structure load='2qcs' size='400' frame='false' align='center' caption='Insert caption here' scene='Insert optional scene name here' />

In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

==Binding to ATP==
Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits. The lopp region that these occur in is referred to as the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'>glycine-rich loop</scene>. Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. <ref>PMID: 9202006</ref>

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T22:10:18Z

Andrew Menke:

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref> The N-terminus of the catalytic subunit is myristylated, although this is not shown in the electron density of this crystal structure. The myristylation does not confer membrane localization but stabilizes the enzyme to denaturation by a factor of 5. <ref>PMID: 8428909</ref>

==Activation and Interaction with Regulatory Subunit==
[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

<Structure load='2qcs' size='400' frame='false' align='middle' caption='Insert caption here' scene='Insert optional scene name here' />

In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

==Binding to ATP==
Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits. The lopp region that these occur in is referred to as the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'>glycine-rich loop</scene>. Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. <ref>PMID: 9202006</ref>
<Structure load='2jds' size='400' frame='false' align='middle' caption='Insert caption here' scene='Insert optional scene name here' />

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T18:31:09Z

Andrew Menke:

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}
==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref> The N-terminus of the catalytic subunit is myristylated, although this is not shown in the electron density of this crystal structure. The myristylation does not confer membrane localization but stabilizes the enzyme to denaturation by a factor of 5. <ref>PMID: 8428909</ref>

==Activation and Interaction with Regulatory Subunit==
[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

<Structure load='2qcs' size='500' frame='false' align='middle' caption='Insert caption here' scene='Insert optional scene name here' />

In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

==Binding to ATP==
Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits. The lopp region that these occur in is referred to as the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'>glycine-rich loop</scene>. Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP. <ref>PMID: 9202006</ref>
<Structure load='2jds' size='500' frame='false' align='left' caption='Insert caption here' scene=Gly-atp-close/1' />

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T18:29:03Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T18:27:14Z

Andrew Menke:

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}
==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref> The N-terminus of the catalytic subunit is myristylated, although this is not shown in the electron density of this crystal structure. The myristylation does not confer membrane localization but stabilizes the enzyme to denaturation by a factor of 5. <ref>PMID: 8428909</ref>

==Activation and Interaction with Regulatory Subunit==
[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

<Structure load='2qcs' size='500' frame='false' align='middle' caption='Insert caption here' scene='Insert optional scene name here' />

In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

==Binding to ATP==
<Structure load='2jds' size='500' frame='true' align='right' caption='Insert caption here' scene=Gly-atp-far/1' />
Typical kinases are characterized by 3 highly conserved glycine residues located near the junction between the small and large kinase subunits. The lopp region that these occur in is referred to as the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Gly-atp-close/1'>glycine-rich loop</scene>. Mutation of any of these residues results in dramatic reduction of kinase affinity for ATP.

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T18:15:04Z

Andrew Menke:

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}
==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref> The N-terminus of the catalytic subunit is myristylated, although this is not shown in the electron density of this crystal structure. The myristylation does not confer membrane localization but stabilizes the enzyme to denaturation by a factor of 5. <ref>PMID: 8428909</ref>

==Activation and Interaction with Regulatory Subunit==
[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

<Structure load='2qcs' size='500' frame='false' align='middle' caption='Insert caption here' scene='Insert optional scene name here' />

In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

==Binding to ATP==
<Structure load='2jds' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T14:16:55Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T14:13:14Z

Andrew Menke:

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}
==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref>

==Activation and Interaction with Regulatory Subunit==
[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

<Structure load='2qcs' size='500' frame='false' align='middle' caption='Insert caption here' scene='Insert optional scene name here' />

In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T14:12:30Z

Andrew Menke:

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}
==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref>

==Activation and Interaction with Regulatory Subunit==
[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

<Structure load='2qcs' size='500' frame='false' align='center' caption='Insert caption here' scene='Insert optional scene name here' />

In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T14:11:55Z

Andrew Menke:

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}
==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene> <ref>PMID: 8167567</ref>

==Activation and Interaction with Regulatory Subunit==
[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

<Structure load='2qcs' size='500' frame='false' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation. <ref>PMID: 17889648</ref> <ref>PMID: 3356685
</ref>

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T14:10:01Z

Andrew Menke:

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}
==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene>

==Activation and Interaction with Regulatory Subunit==
[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

<Structure load='2qcs' size='500' frame='false' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation.<ref>PMID: 17889648</ref>.<ref>PMID: 3356685
</ref>

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T14:06:05Z

Andrew Menke:

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}
==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene>

==Activation and Interaction with Regulatory Subunit==
[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

<Structure load='2qcs' size='500' frame='false' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation.<ref>PMID: 17889648</ref>

==References==
<references />

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-09T14:00:14Z

Andrew Menke:

==Introduction==
The catalytic subunit of PKA is model kinase that is very well characterized because of its catalytic and structural simplicity and ease of Isolation. PKA is essential to cellular signalling in eukaryotes and is involved in a myriad of different processes depending on cell type. PKA catalyzes the transfer of a gamma-phosphoryl group of a molecule of ATP to either a serine or threonine residue on the target protein. This post-translational modification can serve to alter the function of the phosphorylated target protein.

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}
==General Domain Structure==
The catallytic subunit of PKA consists of a <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-cartoon/1'>bilobal kinase fold</scene> that is characteristic of many kinases throughout nature. The upper N-terminal lobe of the kinase is dominated by beta-sheet architecture while the lower, larger C-term is mostly alpha helical. Located in between the two lobes is the <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Apo-surface/3'>catalytic cleft.</scene>

==Activation and Interaction with Regulatory Subunit==
[[Image:PKA1.svg.png]] [[Image:200px-CAMP.svg.png]]

<Structure load='2qcs' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

In the inactive state, the catalytic subunit of PKA exists as a heterotetramer with two regulatory subunits and two catalytic subunits. Regulatory subunits often interact with A Kinase Anchoring proteins that serve to localize a population of PKA in a certain cellular environment, priming a particular response. Upon, cAMP binding to the regulatory domain of PKA (two molecules of cAMP per regulatory subunit) the catalytic subunit is released from the holoenzyme complex and is free to diffuse and exhibit its catalytic activity. Two of the most important residues for this docking interaction are <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/1'>Trp196</scene> and <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Tyr247/3'>Tyr247</scene> which both sit in the nucleotide binding region (Phosphate Binding Cassette) of the regulatory subunit. In essence, when a cAMP molecule binds to these trp and tyr binding sites, the docking interaction is ablated. This <scene name='CAMP_Dependent_Protein_Kinase,_Catalytic_Subunit/Hydro-contacts/1'>scene</scene> shows a different representation.

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-08T16:02:19Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-08T16:00:28Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-08T15:46:21Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-08T15:41:53Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-06T20:07:10Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-06T20:03:37Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-06T20:02:59Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-06T20:01:22Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-06T19:50:22Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-06T16:34:25Z

Andrew Menke:

File:200px-CAMP.svg.png

2011-05-06T16:33:31Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-06T16:32:32Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-06T16:31:41Z

Andrew Menke:

File:PKA1.svg.png

2011-05-06T16:30:32Z

Andrew Menke: Method of PKA activation.

Method of PKA activation.

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-06T16:29:01Z

Andrew Menke:

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-06T15:26:23Z

Andrew Menke:

==Introduction==
The catalytic subunit of PKA is very well characterized because of its simplicity and ease of Isolation.

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-05T19:52:58Z

Andrew Menke:

==Introduction==
The catalytic subunit of PKA is very well characterized because of its simplicity and ease of Isolation.

Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
and display another structure.

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}

CAMP Dependent Protein Kinase, Catalytic Subunit

2011-05-05T18:33:01Z

Andrew Menke: New page: ==This is a placeholder== This is a placeholder text to help you get started in placing a Jmol applet on your page. At any time, click "Show Preview" at the bottom of this page to see how...

==This is a placeholder==
This is a placeholder text to help you get started in
placing a Jmol applet on your page. At any time, click
"Show Preview" at the bottom of this page to see how it goes.

Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load
and display another structure.

{{STRUCTURE_1j3h | PDB=1j3h | SCENE= }}