Proteopedia - User contributions [en]

Amanda Hussey/Sandbox 1

2011-12-07T18:16:17Z

Amanda Hussey:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].


<Structure load='3kg2' size='[450,338]' frame='true' align='right' caption='Rat glutamate receptor 2 complex with competitive agonist [[3kg2]]' scene='Insert optional scene name here' />
=== Glutamate Receptor ===

The AMPA glutamate receptor is a transmembrane protein located primarily at synapses that plays a critical role in communication between neurons. Our lab is interested in the AMPA receptor because strong evidence suggests that changes in location and amount of AMPA receptors at the synapse are central to learning and memory formation. At a molecular level, formation of memory is thought to be governed by changes at synapses between neurons in the brain through a process called long-term potentiation (LTP). One of the key changes involved in potentiation of a synapse is AMPA receptor insertion into the synapse and trafficking of receptors from extrasynaptic areas to the synapse. Studying receptor location and trafficking is one approach to better understanding the underlying changes that are linked to memory formation, and this is one of the primary goals of our lab.

AMPA receptors are iontropic glutamate receptors that allow cations, primarily sodium, to enter into the neuron when the receptor is bound to a ligand such as glutamate. The influx of positive ions depolarizes the membrane, bringing it closer to the threshold necessary for firing an action potential and passing the signal along the neuron to neighboring neurons. Each AMPA receptor is made up of some combination of four subunits, GluA1-4 (or GluR1-4), and in an adult brain most of these receptors consist of GluA1 and GluA2 or GluA2 and GluA3, though other combinations are possible. Receptors containing the GluA2 subunit are calcium impermeable. The molecules on this page are a GluA2 homomer, an AMPA receptor made up of four GluA2 subunits, the GluA1 subunit binding terminal, and GluA3.

Full view of the glutamate receptor shows the overall structure (amino-terminal, ligand-binding and transmembrane domains) in both <scene name='User:Mariel_Feliciano/sandbox_1/Full_view_black_background/6'>ribbon</scene>(MF) and <scene name='User:Mariel_Feliciano/sandbox_1/Full_view_spacefill/2'>spacefilling</scene> models.

Zooming in at the top of the receptor (<scene name='User:Mariel_Feliciano/sandbox_1/Amino_terminal_domains/2'>Amino Terminal Domains</scene>)(RCB) one can view the amino terminal domain, which is a part of the extracellular domain. This domain is implicated in receptor assembly, trafficking, and localization.

Moving toward the bottom of the receptor (<scene name='Molecular_Playground/Glutamate_Receptor/Transmembrane_domains/5'>Transmembrane Domain</scene>) (SM) one can view the transmembrane domain.

This view (<scene name='Molecular_Playground/Glutamate_Receptor/Glu_antagoinist/2'>receptor antagonist</scene>) highlights the area where a receptor antagonist, 2K200225, will bind.

Close up view of the ligand binding site (<scene name='Molecular_Playground/Glutamate_Receptor/Glu_agonist_/2'>Glutamate Binding</scene>)(AH) of the endogenous ligand glutamate.

S1S2J binding site <scene name='Amanda_Hussey/Sandbox_1/S1s2j/1'>clam shell binding site</scene> (AH)

Molecular Playground banner: The glutamate receptor is found in the brain and allows neurons to communicate

==3D structures of glutamate receptors==

[[Glutamate Receptors]]

==Additional Resources==
For additional information, see: [[Alzheimer's Disease]]
<br />

Amanda Hussey/Sandbox 1

2011-12-07T17:59:26Z

Amanda Hussey:

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].


<Structure load='3kg2' size='[450,338]' frame='true' align='right' caption='Rat glutamate receptor 2 complex with competitive agonist [[3kg2]]' scene='Insert optional scene name here' />
=== Glutamate Receptor ===

The AMPA glutamate receptor is a transmembrane protein located primarily at synapses that plays a critical role in communication between neurons. Our lab is interested in the AMPA receptor because strong evidence suggests that changes in location and amount of AMPA receptors at the synapse are central to learning and memory formation. At a molecular level, formation of memory is thought to be governed by changes at synapses between neurons in the brain through a process called long-term potentiation (LTP). One of the key changes involved in potentiation of a synapse is AMPA receptor insertion into the synapse and trafficking of receptors from extrasynaptic areas to the synapse. Studying receptor location and trafficking is one approach to better understanding the underlying changes that are linked to memory formation, and this is one of the primary goals of our lab.

AMPA receptors are iontropic glutamate receptors that allow cations, primarily sodium, to enter into the neuron when the receptor is bound to a ligand such as glutamate. The influx of positive ions depolarizes the membrane, bringing it closer to the threshold necessary for firing an action potential and passing the signal along the neuron to neighboring neurons. Each AMPA receptor is made up of some combination of four subunits, GluA1-4 (or GluR1-4), and in an adult brain most of these receptors consist of GluA1 and GluA2 or GluA2 and GluA3, though other combinations are possible. Receptors containing the GluA2 subunit are calcium impermeable. The molecules on this page are a GluA2 homomer, an AMPA receptor made up of four GluA2 subunits, the GluA1 subunit binding terminal, and GluA3.

Full view of the glutamate receptor shows the overall structure (amino-terminal, ligand-binding and transmembrane domains) in both <scene name='User:Mariel_Feliciano/sandbox_1/Full_view_black_background/6'>ribbon</scene>(MF) and <scene name='User:Mariel_Feliciano/sandbox_1/Full_view_spacefill/2'>spacefilling</scene> models.

Zooming in at the top of the receptor (<scene name='User:Mariel_Feliciano/sandbox_1/Amino_terminal_domains/2'>Amino Terminal Domains</scene>)(RCB) one can view the amino terminal domain, which is a part of the extracellular domain. This domain is implicated in receptor assembly, trafficking, and localization.

Moving toward the bottom of the receptor (<scene name='Molecular_Playground/Glutamate_Receptor/Transmembrane_domains/5'>Transmembrane Domain</scene>) (SM) one can view the transmembrane domain.

This view (<scene name='Molecular_Playground/Glutamate_Receptor/Glu_antagoinist/2'>receptor antagonist</scene>) highlights the area where a receptor antagonist, 2K200225, will bind.

Close up view of the ligand binding site (<scene name='Molecular_Playground/Glutamate_Receptor/Glu_agonist_/2'>Glutamate Binding</scene>)(AH) of the endogenous ligand glutamate.

S1S2J binding site (<scene name='Amanda_Hussey/Sandbox_1/S1s2j_site/1'>S1S2J site</scene>) (AH)

Molecular Playground banner: The glutamate receptor is found in the brain and allows neurons to communicate

==3D structures of glutamate receptors==

[[Glutamate Receptors]]

==Additional Resources==
For additional information, see: [[Alzheimer's Disease]]
<br />

Amanda Hussey/Sandbox 1

2011-12-07T17:42:57Z

Amanda Hussey: content edit

One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].


<Structure load='3kg2' size='[450,338]' frame='true' align='right' caption='Rat glutamate receptor 2 complex with competitive agonist [[3kg2]]' scene='Insert optional scene name here' />
=== Glutamate Receptor ===

The AMPA glutamate receptor is a transmembrane protein located primarily at synapses that plays a critical role in communication between neurons. Our lab is interested in the AMPA receptor because strong evidence suggests that changes in location and amount of AMPA receptors at the synapse are central to learning and memory formation. At a molecular level, formation of memory is thought to be governed by changes at synapses between neurons in the brain through a process called long-term potentiation (LTP). One of the key changes involved in potentiation of a synapse is AMPA receptor insertion into the synapse and trafficking of receptors from extrasynaptic areas to the synapse. Studying receptor location and trafficking is one approach to better understanding the underlying changes that are linked to memory formation, and this is one of the primary goals of our lab.

AMPA receptors are iontropic glutamate receptors that allow cations, primarily sodium, to enter into the neuron when the receptor is bound to a ligand such as glutamate. The influx of positive ions depolarizes the membrane, bringing it closer to the threshold necessary for firing an action potential and passing the signal along the neuron to neighboring neurons. Each AMPA receptor is made up of some combination of four subunits, GluA1-4 (or GluR1-4), and in an adult brain most of these receptors consist of GluA1 and GluA2 or GluA2 and GluA3, though other combinations are possible. Receptors containing the GluA2 subunit are calcium impermeable. The molecules on this page are a GluA2 homomer, an AMPA receptor made up of four GluA2 subunits, the GluA1 subunit binding terminal, and GluA3.

Full view of the glutamate receptor shows the overall structure (amino-terminal, ligand-binding and transmembrane domains) in both <scene name='User:Mariel_Feliciano/sandbox_1/Full_view_black_background/6'>ribbon</scene>(MF) and <scene name='User:Mariel_Feliciano/sandbox_1/Full_view_spacefill/2'>spacefilling</scene> models.

Zooming in at the top of the receptor (<scene name='User:Mariel_Feliciano/sandbox_1/Amino_terminal_domains/2'>Amino Terminal Domains</scene>)(RCB) one can view the amino terminal domain, which is a part of the extracellular domain. This domain is implicated in receptor assembly, trafficking, and localization.

Moving toward the bottom of the receptor (<scene name='Molecular_Playground/Glutamate_Receptor/Transmembrane_domains/5'>Transmembrane Domain</scene>) (SM) one can view the transmembrane domain.

This view (<scene name='Molecular_Playground/Glutamate_Receptor/Glu_antagoinist/2'>receptor antagonist</scene>) highlights the area where a receptor antagonist, 2K200225, will bind.

Close up view of the ligand binding site (<scene name='Molecular_Playground/Glutamate_Receptor/Glu_agonist_/2'>Glutamate Binding</scene>)(AH) of the endogenous ligand glutamate.

Molecular Playground banner: The glutamate receptor is found in the brain and allows neurons to communicate

==3D structures of glutamate receptors==

[[Glutamate Receptors]]

==Additional Resources==
For additional information, see: [[Alzheimer's Disease]]
<br />

Molecular Playground/Glutamate Receptor

2010-04-30T18:38:51Z

Amanda Hussey:

A [[CBI Molecule]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].

<applet size='[450,338]' frame='true' align='right'
caption='Glutamate Receptor' />

=== Glutamate Receptor ===

The AMPA glutamate receptor is a transmembrane protein located primarily at synapses that plays a critical role in communication between neurons. Our lab is interested in the AMPA receptor because strong evidence suggests that changes in location and amount of AMPA receptors at the synapse are central to learning and memory formation. At a molecular level, formation of memory is thought to be governed by changes at synapses between neurons in the brain through a process called long-term potentiation (LTP). One of the key changes involved in potentiation of a synapse is AMPA receptor insertion into the synapse and trafficking of receptors from extrasynaptic areas to the synapse. Studying receptor location and trafficking is one approach to better understanding the underlying changes that are linked to memory formation, and this is one of the primary goals of our lab.

AMPA receptors are iontropic glutamate receptors that allow cations, primarily sodium, to enter into the neuron when the receptor is bound to a ligand such as glutamate. The influx of positive ions depolarizes the membrane, bringing it closer to the threshold necessary for firing an action potential and passing the signal along the neuron to neighboring neurons. Each AMPA receptor is made up of some combination of four subunits, GluR1-4, and in an adult brain most of these receptors consist of GluR1 and Glur2 or Glur2 and Glur3, though other combinations are possible. Receptors containing the GluR2 subunit are calcium impermeable. The molecule on this page is a GluR2 homomer, an AMPA receptor made up of four GluR2 subunits.

Full view of the glutamate receptor shows the overall structure (amino-terminal, ligand-binding and transmembrane domains) in both <scene name='User:Mariel_Feliciano/sandbox_1/Full_view_black_background/6'>ribbon</scene>(MF) and <scene name='User:Mariel_Feliciano/sandbox_1/Full_view_spacefill/2'>spacefilling</scene> models.

Zooming in at the top of the receptor (<scene name='User:Mariel_Feliciano/sandbox_1/Amino_terminal_domains/2'>Amino Terminal Domains</scene>)(RCB) one can view the amino terminal domain, which is a part of the extracellular domain. This domain is implicated in receptor assembly, trafficking, and localization.

Moving toward the bottom of the receptor (<scene name='Molecular_Playground/Glutamate_Receptor/Transmembrane_domains/5'>Transmembrane Domain</scene>) (SM) one can view the transmembrane domain.

This view (<scene name='Molecular_Playground/Glutamate_Receptor/Glu_antagoinist/2'>receptor antagonist</scene>) highlights the area where a receptor antagonist, 2K200225, will bind.

Close up view of the ligand binding site (<scene name='Molecular_Playground/Glutamate_Receptor/Glu_agonist_/2'>Glutamate Binding</scene>)(AH) of the endogenous ligand glutamate.

Molecular Playground banner: The glutamate receptor is found in the brain and allows neurons to communicate

Molecular Playground/Glutamate Receptor

2010-04-30T00:36:31Z

Amanda Hussey:

Molecular Playground/Glutamate Receptor

2010-04-28T19:57:16Z

Amanda Hussey:

Molecular Playground/Glutamate Receptor

2010-04-28T19:56:32Z

Amanda Hussey:

Molecular Playground/Glutamate Receptor

2010-04-28T19:39:58Z

Amanda Hussey:

Molecular Playground/Glutamate Receptor

2010-04-28T19:36:54Z

Amanda Hussey:

Molecular Playground/Glutamate Receptor

2010-04-28T19:33:46Z

Amanda Hussey:

Molecular Playground/Glutamate Receptor

2010-04-28T19:29:34Z

Amanda Hussey:

Molecular Playground/Glutamate Receptor

2010-04-28T19:26:58Z

Amanda Hussey:

Molecular Playground/Glutamate Receptor

2010-04-28T19:25:29Z

Amanda Hussey:

Molecular Playground/Glutamate Receptor

2010-04-28T19:15:29Z

Amanda Hussey:

Molecular Playground/Glutamate Receptor

2010-04-28T19:12:06Z

Amanda Hussey:

Molecular Playground/Glutamate Receptor

2010-04-28T19:10:25Z

Amanda Hussey:

User:Amanda Hussey/Sandbox 1

2010-03-16T15:59:02Z

Amanda Hussey:

<applet size='[450,338]' frame='true' align='right'
caption='YYY' />

<scene name='User:Amanda_Hussey/Sandbox_1/Rrr/2'>TextToBeDisplayed</scene>

<scene name='User:Amanda_Hussey/Sandbox_1/Rrr/3'>TextToBeDisplayed</scene>

<scene name='User:Amanda_Hussey/Sandbox_1/Rrr/4'>scene skipping transitions</scene>

<scene name='User:Amanda_Hussey/Sandbox_1/Fjt/1'>TextToBeDisplayed</scene>
*<scene name='User:Amanda_Hussey/Sandbox_1/Fjt/2'>TextToBeDisplayed</scene>

User:Amanda Hussey/Sandbox 1

2010-03-16T15:55:36Z

Amanda Hussey:

User:Amanda Hussey/Sandbox 1

2010-03-16T15:31:13Z

Amanda Hussey:

<applet size='[450,338]' frame='true' align='right'
caption='YYY' />

<scene name='User:Amanda_Hussey/Sandbox_1/Glur2/1'>TextToBeDisplayed</scene>;
<scene name='User:Amanda_Hussey/Sandbox_1/Glur2/2'>TextToBeDisplayed</scene>;
<scene name='User:Amanda_Hussey/Sandbox_1/Glur2/3'>TextToBeDisplayed</scene>;

<scene name='User:Amanda_Hussey/Sandbox_1/Rrr/2'>TextToBeDisplayed</scene>

<scene name='User:Amanda_Hussey/Sandbox_1/Rrr/3'>TextToBeDisplayed</scene>

<scene name='User:Amanda_Hussey/Sandbox_1/Rrr/4'>scene skipping transitions</scene>

User:Amanda Hussey/Sandbox 1

2010-03-16T15:27:35Z

Amanda Hussey:

<applet size='[450,338]' frame='true' align='right'
caption='YYY' />

<scene name='User:Amanda_Hussey/Sandbox_1/Glur2/1'>TextToBeDisplayed</scene>;
<scene name='User:Amanda_Hussey/Sandbox_1/Glur2/2'>TextToBeDisplayed</scene>;
<scene name='User:Amanda_Hussey/Sandbox_1/Glur2/3'>TextToBeDisplayed</scene>;

<scene name='User:Amanda_Hussey/Sandbox_1/Rrr/2'>TextToBeDisplayed</scene>;
<scene name='User:Amanda_Hussey/Sandbox_1/Rrr/3'>TextToBeDisplayed</scene>

User:Amanda Hussey/Sandbox 1

2010-03-16T15:25:34Z

Amanda Hussey:

User:Amanda Hussey/Sandbox 1

2010-03-16T15:10:39Z

Amanda Hussey:

User:Amanda Hussey/Sandbox 1

2010-03-16T15:07:27Z

Amanda Hussey:

<applet size='[450,338]' frame='true' align='right'
caption='YYY' />

<scene name='User:Amanda_Hussey/Sandbox_1/Glur2/1'>TextToBeDisplayed</scene>
<scene name='User:Amanda_Hussey/Sandbox_1/Glur2/2'>TextToBeDisplayed</scene>

User:Amanda Hussey/Sandbox 1

2010-03-16T14:47:48Z

Amanda Hussey:

<applet size='[450,338]' frame='true' align='right'
caption='YYY' />

<scene name='User:Amanda_Hussey/Sandbox_1/Glur2/1'>TextToBeDisplayed</scene>

User:Amanda Hussey/Sandbox 1

2010-03-16T14:33:08Z

Amanda Hussey: New page: <applet size='[450,338]' frame='true' align='right' caption='YYY' />