Sandbox Reserved 691
From Proteopedia
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= Dopamine Active Transporter = | = Dopamine Active Transporter = | ||
Dopamine Active Transporter (DAT) is a transmembrane protein found in human neurons, that is responsible for the reuptake of the neurotransmitter dopamine from the synapse back into synaptic vesicles for storage and later release. The action of this protein is responsible for the termination of signaling in dopaminergic pathways, which are responsible for many important biological functions such as cognition, motor control, sleep, and emotion. | Dopamine Active Transporter (DAT) is a transmembrane protein found in human neurons, that is responsible for the reuptake of the neurotransmitter dopamine from the synapse back into synaptic vesicles for storage and later release. The action of this protein is responsible for the termination of signaling in dopaminergic pathways, which are responsible for many important biological functions such as cognition, motor control, sleep, and emotion. | ||
| - | <Structure load='2a65' size='500' frame='true' align='right' caption='LEUTAA, a bacterial homolog for human Na+/Cl- dependent neurotransmitter transporters such as DAT' scene='' /> | + | <Structure load='2a65' size='500' frame='true' align='right' caption='LEUTAA, a bacterial homolog for human Na+/Cl- dependent neurotransmitter transporters such as DAT' scene='Sandbox_Reserved_691/2a65_default/2' /> |
== Function == | == Function == | ||
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Amphetamines are a class of chemical compounds derived from amphetamine ((RS)-1-phenylpropan-2-amine) and are used both recreationally to induce euphoria and clinically to treat disorders, notably Attention Deficit Hyperactivity Disorder (ADHD). While amphetamines bear structural similarities to dopamine, they are not true competitive inhibitors of the dopamine transporter. Amphetamines instead work by binding to an unknown receptor that initiates phosphorylation of the N-terminus once Ca2+/calmodulin-dependent protein kinase II (CamKII) binds to the C-terminus. This causes DAT to conform to a "willing" conformation and results in DAT effluxing into the cell through the formation of an intercellular endosome. This reduces the expression of DAT in the surface of the cell membrane, reducing the rate at which dopamine is cleared from the synapse. | Amphetamines are a class of chemical compounds derived from amphetamine ((RS)-1-phenylpropan-2-amine) and are used both recreationally to induce euphoria and clinically to treat disorders, notably Attention Deficit Hyperactivity Disorder (ADHD). While amphetamines bear structural similarities to dopamine, they are not true competitive inhibitors of the dopamine transporter. Amphetamines instead work by binding to an unknown receptor that initiates phosphorylation of the N-terminus once Ca2+/calmodulin-dependent protein kinase II (CamKII) binds to the C-terminus. This causes DAT to conform to a "willing" conformation and results in DAT effluxing into the cell through the formation of an intercellular endosome. This reduces the expression of DAT in the surface of the cell membrane, reducing the rate at which dopamine is cleared from the synapse. | ||
| - | <scene name='Sandbox_Reserved_691/2a65_default/ | + | <scene name='Sandbox_Reserved_691/2a65_default/2'>DEFAULT</scene> |
| - | <scene name='Sandbox_Reserved_691/2a65_ions/ | + | <scene name='Sandbox_Reserved_691/2a65_ions/2'>IONS</scene> |
<scene name='Sandbox_Reserved_691/2a65_leucine/2'>LEUCINE</scene> | <scene name='Sandbox_Reserved_691/2a65_leucine/2'>LEUCINE</scene> | ||
| - | <scene name='Sandbox_Reserved_691/ | + | <scene name='Sandbox_Reserved_691/2a65_hydrogen/2'>HBOND</scene> |
| - | <scene name='Sandbox_Reserved_691/ | + | <scene name='Sandbox_Reserved_691/2a65_hydrophilphob/1'>HYDROPHILPHOB</scene> |
| + | |||
| + | <scene name='Sandbox_Reserved_691/2a65_secondary/2'>SECONDARY</scene> | ||
<scene name='Sandbox_Reserved_691/2a65_water2/1'>SOLVENT ACCESSABILITY</scene> | <scene name='Sandbox_Reserved_691/2a65_water2/1'>SOLVENT ACCESSABILITY</scene> | ||
Revision as of 06:58, 28 April 2013
| This Sandbox is Reserved from 30/01/2013, through 30/12/2013 for use in the course "Biochemistry II" taught by Hannah Tims at the Messiah College. This reservation includes Sandbox Reserved 686 through Sandbox Reserved 700. |
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Dopamine Active Transporter
Dopamine Active Transporter (DAT) is a transmembrane protein found in human neurons, that is responsible for the reuptake of the neurotransmitter dopamine from the synapse back into synaptic vesicles for storage and later release. The action of this protein is responsible for the termination of signaling in dopaminergic pathways, which are responsible for many important biological functions such as cognition, motor control, sleep, and emotion.
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Function
Through the binding of two sodium ions, dopamine can then bind after which the protein undergoes a conformational change to allow for the sodium and dopamine to enter the cell. Similar to other ionic pumps, the flow of sodium is coupled with the flow of a chlorine ion, in order to balance the charge build up. The internalization of dopamine into neural cells allows for the clearing of dopamine from the synapse and the termination of dopamine signaling pathways.
Amphetamines
Amphetamines are a class of chemical compounds derived from amphetamine ((RS)-1-phenylpropan-2-amine) and are used both recreationally to induce euphoria and clinically to treat disorders, notably Attention Deficit Hyperactivity Disorder (ADHD). While amphetamines bear structural similarities to dopamine, they are not true competitive inhibitors of the dopamine transporter. Amphetamines instead work by binding to an unknown receptor that initiates phosphorylation of the N-terminus once Ca2+/calmodulin-dependent protein kinase II (CamKII) binds to the C-terminus. This causes DAT to conform to a "willing" conformation and results in DAT effluxing into the cell through the formation of an intercellular endosome. This reduces the expression of DAT in the surface of the cell membrane, reducing the rate at which dopamine is cleared from the synapse.
