Sandbox Reserved 1714 - Revision history

Courtney Vennekotter at 05:08, 19 April 2022

Courtney Vennekotter — Tue, 19 Apr 2022 05:08:23 GMT

←Older revision		Revision as of 05:08, 19 April 2022
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	'''3.''' A second glutamate then binds to the other <scene name='90/904320/Active_site_interactions/4'>binding pocket</scene> of the VFT. Mediated by L639, F643, N735, W773, and F776, a <scene name='90/904320/Pam/8'>positive allosteric modulator</scene> (PAM) also binds within the seven TMD helices of the alpha chain <ref name="Seven">PMID:34194039</ref>. This closed conformation of the VFT now has an inter-lobe angle of 25° is considered to be in the <scene name='90/904320/Active_mglu/6'>active conformation</scene><ref name="Seven">PMID:34194039</ref>. The binding of these ligands allows the CRDs to compact and come together. This transformation causes the TMD to form a separate, active asymmetric conformation with a <scene name='90/904319/Active_helices/23'>TM6-TM6 interface</scene> between the chains<ref name="Seven">PMID:34194039</ref>.		'''3.''' A second glutamate then binds to the other <scene name='90/904320/Active_site_interactions/4'>binding pocket</scene> of the VFT. Mediated by L639, F643, N735, W773, and F776, a <scene name='90/904320/Pam/8'>positive allosteric modulator</scene> (PAM) also binds within the seven TMD helices of the alpha chain <ref name="Seven">PMID:34194039</ref>. This closed conformation of the VFT now has an inter-lobe angle of 25° is considered to be in the <scene name='90/904320/Active_mglu/6'>active conformation</scene><ref name="Seven">PMID:34194039</ref>. The binding of these ligands allows the CRDs to compact and come together. This transformation causes the TMD to form a separate, active asymmetric conformation with a <scene name='90/904319/Active_helices/23'>TM6-TM6 interface</scene> between the chains<ref name="Seven">PMID:34194039</ref>.

-	'''4.''' The crossover of the helices from the alpha and beta chains allows for intracellular loop 2 (ICL2) and the C-terminus to be properly ordered to interact with a single G protein<ref name="Seven">PMID:34194039</ref>. While hydrogen bonding is present between the C-terminus and alpha helix 5 of the G-protein, this coupling is primarily driven by the hydrophobic interactions in the interface with the ɑ5 helix of the G protein<ref name="Seven">PMID:34194039</ref>(Figure 4). This <scene name='90/904320/Active_mglu/5'>mGlu/G-protein coupling ~~XXXXPAMXXX~~ as the pocket in which the coupling occurs would be completely closed in its absence<ref name="Seven">PMID:34194039</ref>.	+	'''4.''' The crossover of the helices from the alpha and beta chains allows for intracellular loop 2 (ICL2) and the C-terminus to be properly ordered to interact with a single G protein<ref name="Seven">PMID:34194039</ref>. While hydrogen bonding is present between the C-terminus and alpha helix 5 of the G-protein, this coupling is primarily driven by the hydrophobic interactions in the interface with the ɑ5 helix of the G protein<ref name="Seven">PMID:34194039</ref>(Figure 4). This <scene name='90/904320/Active_mglu/5'>mGlu/G-protein coupling PAM as the pocket in which the coupling occurs would be completely closed in its absence<ref name="Seven">PMID:34194039</ref>.

	'''5.''' Upon binding, the G protein can become active through the receptor catalyzed reaction of GDP to GTP on the alpha subunit of the G protein. Depending on the type of mGlu present, this activation causes different signaling cascades to occur within the cell <ref name="Lin">PMID:34135510</ref>. These cascades are necessary for cellular function as they can play primary roles in regulating metabolic molecules, ion channels, transporter molecules, and several other parts of the cell; if these proteins are mutated, various diseases can occur<ref name="Crupi">PMID:30800054</ref>.		'''5.''' Upon binding, the G protein can become active through the receptor catalyzed reaction of GDP to GTP on the alpha subunit of the G protein. Depending on the type of mGlu present, this activation causes different signaling cascades to occur within the cell <ref name="Lin">PMID:34135510</ref>. These cascades are necessary for cellular function as they can play primary roles in regulating metabolic molecules, ion channels, transporter molecules, and several other parts of the cell; if these proteins are mutated, various diseases can occur<ref name="Crupi">PMID:30800054</ref>.

Courtney Vennekotter at 05:06, 19 April 2022

Courtney Vennekotter — Tue, 19 Apr 2022 05:06:35 GMT

←Older revision		Revision as of 05:06, 19 April 2022
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-	~~{{Template:CH462_Biochemistry_II_2022}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->~~	+	__NoTOC__
-	=~~=Your Heading Here (maybe something like 'Structure')=~~=	+	= Metabotropic Glutamate Receptor =
-	<StructureSection load='~~1stp~~' size='340' side='right' caption='~~Caption for this structure~~' scene=''>	+	<StructureSection load='7epa' size='340' side='right' caption='Metabotropic Glutamate Receptor PDB:[http://www.rcsb.org/pdb/explore/explore.do?structureId=7epa 7epa]' scene='90/904320/Inactive_mglu2_first_picture/3'>
-	~~This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.~~	+
-	~~You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002~~/~~ijch.201300024<~~/~~ref> or to the article describing Jmol <ref>PMID:21638687<~~/~~ref~~> ~~to the rescue.~~	+

-	== ~~Function~~ ==	+	== Introduction ==
		+	Within the [https://en.wikipedia.org/wiki/Central_nervous_system central nervous system (CNS)], various membrane receptors exist to detect extracellular signaling molecules and communicate this information intracellularly. Found in eukaryotes and known for its seven transmembrane helices, [https://en.wikipedia.org/wiki/G_protein-coupled_receptor G-protein coupled receptor] (GPCR) are one type of membrane bound receptors with conserved intracellular signaling via heterotrimeric [https://en.wikipedia.org/wiki/G_protein#:~:text=G%20proteins%2C%20also%20known%20as,a%20cell%20to%20its%20interior. G-protein]<ref name="Katritch">PMID:23140243</ref>. The metabotropic glutamate receptor (mGlu), a Class C GPCR, is a receptor utilized in glutamate signaling- which is essential in synaptic plasticity as well as the development and repair of the CNS<ref name="Niswender">PMID:20055706</ref>. These receptors are specifically found in the pre- and postsynaptic [https://en.wikipedia.org/wiki/Neuron#:~:text=A%20neuron%20or%20nerve%20cell,animals%20except%20sponges%20and%20placozoa. neurons] of the CNS<ref name="Niswender">PMID:20055706</ref>. Eight different mGlu subtypes exist which are divided into three groups (I, II, III)<ref name="Niswender">PMID:20055706</ref>. While each mGlu has a slightly different function and location, the structures of the different mGlu subtypes are very similar (Table 1) <ref name="Niswender">PMID:20055706</ref>. For each group, binding of the [https://en.wikipedia.org/wiki/Glutamate_(neurotransmitter) neurotransmitter glutamate] to the mGlu introduces a conformational change that can activate a G-protein<ref name="Niswender">PMID:20055706</ref>.

-	== ~~Disease~~ ==	+	{\| class="wikitable" style="text-align:center;"
		+	\|-
		+	! colspan="4" style="font-weight:bold;" \| Table 1. Classification of mGlu Subtypes<ref name="Niswender">PMID:20055706</ref>
		+	\|- style="font-weight:bold;"
		+	\| Group
		+	\| mGlu Type
		+	\| Location
		+	\| Function
		+	\|- style="background-color:#ffffff;"
		+	\| I
		+	\| mGlu1<br />mGlu5
		+	\| Postsynaptic neurons
		+	\| Activates calcium channels<br />Excites adenylyl cyclase
		+	\|- style="background-color:#ffffff;"
		+	\| II
		+	\| mGlu2<br />mGlu3
		+	\| Presynaptic neurons
		+	\| Activates potassium channels<br />Inhibits calcium channels<br />Inhibits adenylyl cyclase
		+	\|- style="background-color:#ffffff;"
		+	\| III
		+	\| mGlu4<br />mGlu6<br />mGlu7<br />mGlu8
		+	\| Presynaptic neurons
		+	\| Activates potassium channels<br />Inhibits calcium channels<br />Inhibits adenylyl cyclase
		+	\|}

-	== ~~Relevance~~ ==	+	[[Image:Glutamate.png\|300 px\|right\|thumb\|Figure 1. Structure of glutamate under physiological conditions (pH 7.4).]] To activate the mGlu transformation, glutamate acts as the protein's main agonist. Glutamate is an acidic, polar amino acid (Figure 1). This agonist binds to the extracellular portion of the glutamate receptor causing the transmembrane spanning region of the homodimer to change conformationally. This change allows for the mGlu to bind to a G-protein. This binding allows for the activation of a G protein which initiates a signaling cascade within the cell that can ultimately lead to a difference in the synapse’s excitability<ref name="Seven">PMID:34194039</ref>. In mGlu, the binding affinity of glutamate is also controlled by the binding of either a positive (PAM) or negative (NAM) allosteric modulator to a binding pocket within the seven TMD<ref name="Lin">PMID:34135510</ref>.
		+	== Structural Highlights ==
		+	mGlu receptors are dimeric proteins consisting of an <scene name='90/904320/Inactive_mglu2/11'>alpha and beta chain</scene>. While a heterodimer of different mGlu subtypes can form, only homodimeric receptors can become active<ref name="Seven">PMID:34194039</ref>. Both the alpha and beta chains are comprised of <scene name='90/904320/Mglu2_domains/8'>three domains</scene>: the venus fly trap (VFT), cysteine rich domain (CRD), and the transmembrane domain (TMD).

-	== ~~Structural highlights~~ ==	+	[[Image: Orientation_2.png\|250px\|left\|thumb\|Figure 2. Proper orientation of mGlu about the cell membrane.]]
-	<scene name='90/904319/~~Pam~~/1'>~~PAM~~</scene>	+	==== Domains ====
		+	<scene name='90/904320/Mglu2_domains_vft/3'>VFT</scene>: The extracellular location in which the two glutamate agonists bind is known as the VFT. This domain includes a disulfide bond between C121 of the alpha and beta chains. This <scene name='90/904320/Inactive_mglu/8'>inactive dimer disulfide bond</scene> is shifted down and undergoes an <scene name='90/904319/Cys_active/1'>upward movement</scene> upon glutamate binding which stabilizes the <scene name='90/904320/Active_site_interactions/4'>active site</scene> (Figure 2) Glutamate binds within the <scene name='90/904320/Active_site_interactions/3'>binding pocket</scene> through intermolecular forces, specifically hydrogen bonding, with R57, S143, S145, T168, and K377 of the VFT. This binding initiates a closed VFT conformation.

-	<scene name='90/~~904319~~/~~Pam_binding~~/2'>~~PAM Binding~~</scene>	+	<scene name='90/904320/Mglu2_domains_crd/3'>CRD</scene>: The portion of the protomer that connects the VFT with the TMD is known as the CRD. Many <scene name='90/904320/Crd_cysteine/3'>disulfide bonds</scene> are located in this region between cysteines. As the connecting segment of the protein, it is critical in transmitting the conformational change caused by the binding of glutamate to the TMD. The change resulting from the binding of glutamate in the VFT brings the cysteine-rich domains pf the alpha and beta chain together to alter the configuration of the the seven TMD helices through its interaction with the VFT extracellular loop 2 (ECL2) <ref name="Seven">PMID:34194039</ref>. This <scene name='90/904320/Active_helices/11'>ECL2 conformational change</scene> is mediated through interactions with amino acids at the apex of the CRD (e.g. I <ref name="Seven">PMID:34194039</ref>.

-	<scene name='90/904319/Active_helices/8'>~~Crossover~~</scene>	+	<scene name='90/904320/Mglu2_domains_tmd/5'>TMD</scene>: The TMD consists of <scene name='90/904319/Inactive_tmd/9'>7 transmembrane helices</scene> that are responsible for G-protein interactions and are able to transmit the signal from ligand binding across a membrane. In the <scene name='90/904320/Inactive_mglu/4'>inactive form</scene>, the asymmetric conformation of the helices is mediated by the hydrophobicity of helix 3 and 4 <ref name="Seven">PMID:34194039</ref>. This allows for a <scene name='90/904319/Inactive_tmd_interface/7'>TM3/TM4 interface</scene> to form between the monomers. Along with the interaction of the CRD with the ECL2 of the TMD, an allosteric modulator must bind within the transmembrane helices to allow for the conformation of the helices to be altered. This conformation allows for an <scene name='90/904319/Active_helices/23'>active dimer interface</scene> along helix 6 of both protomers <ref name="Lin">PMID:34135510</ref>. The stabilization of this conformation also enables G protein coupling with ICL2, ICL3, TM Helix 3 and the C terminus <ref name="Lin">PMID:34135510</ref> (Figure 4).

-	~~This~~ is ~~a sample scene created with SAT to~~ <scene name="/12/~~3456~~/~~Sample/1"~~>~~color~~</scene> ~~by Group~~, ~~and another to make~~ <~~scene~~ name="~~/12/3456/Sample/2~~">~~a transparent representation~~</~~scene~~> ~~of the protein~~. ~~You can make your own scenes on SAT starting from scratch or loading~~ and ~~editing one of these sample scenes~~.	+	== Conformational Changes ==
		+	[[Image:Overview_mGlu_2.jpg\|900 px\|center\|thumb\|Figure 3. Illustration of mGlu's conformational change process.]]
		+	'''1.''' In its resting state, mGlu is in an <scene name='90/904320/Inactive_mglu/4'>inactive homodimeric form</scene>. In this conformation, the receptor is considered open with an inter-lobe angle of 44°<ref name="Seven">PMID:34194039</ref>. The structure has two free glutamate binding sites in the VFT, the CRDs are separated, and the TMD is not interacting with a G protein<ref name="Seven">PMID:34194039</ref>.

-	~~NEW SCENES~~	+	'''2.''' In the intermediate activation state, also known as the open-closed conformation, one glutamate is bound in one binding pocket of VFT. This single <scene name='90/904320/Mglu_binding/8'>glutamate bound state</scene> is still considered inactive as the receptor has not changed the conformations in the CRD and thus the TMD. With the same asymmetric transmembrane helices formation, a <scene name='90/904319/Inactive_tmd_interface/7'>TM3/TM4 interface</scene> is still present and mGlu cannot interact with a G protein<ref name="Seven">PMID:34194039</ref>.
-	<scene name='90/904319/~~Active_helices~~/12'>~~TM6 Interface~~</scene>	+

-	<scene name='90/904319/~~Active_helices_numbered~~/1'>~~Active Helices~~</scene>	+	[[Image:Screen Shot 2022-04-18 at 10.20.26 PM.png\|300 px\|right\|thumb\|Figure 4. The interaction between an active mGlu (magenta/lime/purple/crimson) and a G-protein (orange). Hydrogen bonds are shown through black dashes]]
		+	'''3.''' A second glutamate then binds to the other <scene name='90/904320/Active_site_interactions/4'>binding pocket</scene> of the VFT. Mediated by L639, F643, N735, W773, and F776, a <scene name='90/904320/Pam/8'>positive allosteric modulator</scene> (PAM) also binds within the seven TMD helices of the alpha chain <ref name="Seven">PMID:34194039</ref>. This closed conformation of the VFT now has an inter-lobe angle of 25° is considered to be in the <scene name='90/904320/Active_mglu/6'>active conformation</scene><ref name="Seven">PMID:34194039</ref>. The binding of these ligands allows the CRDs to compact and come together. This transformation causes the TMD to form a separate, active asymmetric conformation with a <scene name='90/904319/Active_helices/23'>TM6-TM6 interface</scene> between the chains<ref name="Seven">PMID:34194039</ref>.

-	<scene name='90/~~904319~~/~~Inactive_tmd~~/5'>~~TMD~~</~~scene~~>	+	'''4.''' The crossover of the helices from the alpha and beta chains allows for intracellular loop 2 (ICL2) and the C-terminus to be properly ordered to interact with a single G protein<ref name="Seven">PMID:34194039</ref>. While hydrogen bonding is present between the C-terminus and alpha helix 5 of the G-protein, this coupling is primarily driven by the hydrophobic interactions in the interface with the ɑ5 helix of the G protein<ref name="Seven">PMID:34194039</ref>(Figure 4). This <scene name='90/904320/Active_mglu/5'>mGlu/G-protein coupling XXXXPAMXXX as the pocket in which the coupling occurs would be completely closed in its absence<ref name="Seven">PMID:34194039</ref>.

-	<~~scene~~ name=~~'90/904319/Inactive_tmd_interface/2'~~>~~TM4~~/~~TM2 Interface~~</~~scene~~>	+	'''5.''' Upon binding, the G protein can become active through the receptor catalyzed reaction of GDP to GTP on the alpha subunit of the G protein. Depending on the type of mGlu present, this activation causes different signaling cascades to occur within the cell <ref name="Lin">PMID:34135510</ref>. These cascades are necessary for cellular function as they can play primary roles in regulating metabolic molecules, ion channels, transporter molecules, and several other parts of the cell; if these proteins are mutated, various diseases can occur<ref name="Crupi">PMID:30800054</ref>.

-	~~FIXED:~~	+	== Clinical Relevance ==
-	<~~scene~~ name='90/~~904319~~/~~Inactive_tmd_interface~~/5'>~~inactive interface~~</~~scene~~> ~~DONE~~	+	Glutamate is a major neurotransmitter in the brain and is known for its role in memory, synaptic plasticity, and neuronal development<ref name="Crupi">PMID:30800054</ref>. Thus, mGlus are located throughout the CNS and play key roles in various neurodegenerative diseases such as [https://en.wikipedia.org/wiki/Alzheimer%27s_disease Alzheimer's Disease] (AD), [https://en.wikipedia.org/wiki/Huntington%27s_disease Huntington's Disease] (HD), [https://en.wikipedia.org/wiki/Parkinson%27s_disease Parkinson’s Disease] (PD), and [https://en.wikipedia.org/wiki/Amyotrophic_lateral_sclerosis Amyotrophic Lateral Sclerosis] (ALS)<ref name="Crupi">PMID:30800054</ref>. Also, due to the key role of glutamate in the brain, mGlus are also being studied for their role in psychiatric disorders like [https://en.wikipedia.org/wiki/Anxiety anxiety] and [https://en.wikipedia.org/wiki/Depression_(mood) depression]<ref name="Crupi">PMID:30800054</ref>. In many of these diseases, the overexpression of glutamate can lead to the overstimulation of mGlus and excitotoxicity <ref name="Bordi">PMID:10416961</ref>. However, an exception to this is the under stimulation of mGlus which can result in schizophrenia<ref name="Conn">PMID:19058862</ref>. Research is ongoing, but studies have proven that agonists, antagonists, PAMs, and NAMs of mGlus are potential treatments for these diseases<ref name="Crupi">PMID:30800054</ref>.

-	~~<scene name~~=~~'90~~/~~904319~~/~~Active_helices~~/~~23'~~>~~TM6 interface~~</~~scene~~> ~~DONE~~	+	== 3D Structures ==
		+	[[7epa]], mGlu Inactive <br />
		+	[[7mtr]], mGlu Active <br />
		+	[[7epb]], mGlu Active <br />
		+	[[7mts]], mGlu Active G Protein Bound <br />

-	<scene name='90/904319/Vft/1'>Glutamate binding site</scene>
-	<scene name='90/904319/Cys_active/1'>upward shift</scene>
-
-	</StructureSection>
	== References ==		== References ==
	<references/>		<references/>
		+
		+	</StructureSection>
		+
		+	== Student Contributors ==
		+	*Courtney Vennekotter
		+	*Cade Chezem

Courtney Vennekotter at 03:13, 19 April 2022

Courtney Vennekotter — Tue, 19 Apr 2022 03:13:19 GMT

←Older revision		Revision as of 03:13, 19 April 2022
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	<scene name='90/904319/Vft/1'>Glutamate binding site</scene>		<scene name='90/904319/Vft/1'>Glutamate binding site</scene>
		+	<scene name='90/904319/Cys_active/1'>upward shift</scene>

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Courtney Vennekotter at 19:24, 15 April 2022

Courtney Vennekotter — Fri, 15 Apr 2022 19:24:48 GMT

←Older revision		Revision as of 19:24, 15 April 2022
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	<scene name='90/904319/Active_helices/23'>TM6 interface</scene> DONE		<scene name='90/904319/Active_helices/23'>TM6 interface</scene> DONE

		+	<scene name='90/904319/Vft/1'>Glutamate binding site</scene>

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Courtney Vennekotter at 16:40, 15 April 2022

Courtney Vennekotter — Fri, 15 Apr 2022 16:40:24 GMT

←Older revision		Revision as of 16:40, 15 April 2022
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	FIXED:		FIXED:
-	<scene name='90/904319/Inactive_tmd_interface/5'>inactive interface</scene>	+	<scene name='90/904319/Inactive_tmd_interface/5'>inactive interface</scene> DONE

-	<scene name='90/904319/Active_helices/18'>TM6 interface</scene>	+	<scene name='90/904319/Active_helices/23'>TM6 interface</scene> DONE

-	<scene name='90/904319/Active_helices/23'>TM6 interface</scene>

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Courtney Vennekotter at 16:19, 15 April 2022

Courtney Vennekotter — Fri, 15 Apr 2022 16:19:24 GMT

←Older revision		Revision as of 16:19, 15 April 2022
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	<scene name='90/904319/Active_helices/18'>TM6 interface</scene>		<scene name='90/904319/Active_helices/18'>TM6 interface</scene>

-	<scene name='90/904319/Active_helices/22'>TM6 interface</scene>	+	<scene name='90/904319/Active_helices/23'>TM6 interface</scene>
		+
	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Courtney Vennekotter at 16:18, 15 April 2022

Courtney Vennekotter — Fri, 15 Apr 2022 16:18:12 GMT

←Older revision		Revision as of 16:18, 15 April 2022
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	<scene name='90/904319/Active_helices/18'>TM6 interface</scene>		<scene name='90/904319/Active_helices/18'>TM6 interface</scene>

		+	<scene name='90/904319/Active_helices/22'>TM6 interface</scene>
	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Courtney Vennekotter at 14:07, 15 April 2022

Courtney Vennekotter — Fri, 15 Apr 2022 14:07:51 GMT

←Older revision		Revision as of 14:07, 15 April 2022
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	FIXED:		FIXED:
-	<scene name='90/904319/Inactive_tmd_interface/4'>~~TM3/TM4~~ interface</scene>	+	<scene name='90/904319/Inactive_tmd_interface/5'>inactive interface</scene>

-	<scene name='90/904319/Active_helices/17'>TM6 interface</scene>	+	<scene name='90/904319/Active_helices/18'>TM6 interface</scene>

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Courtney Vennekotter at 14:05, 15 April 2022

Courtney Vennekotter — Fri, 15 Apr 2022 14:05:51 GMT

←Older revision		Revision as of 14:05, 15 April 2022
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	FIXED:		FIXED:
-	<scene name='90/904319/Inactive_tmd_interface/3'>~~TMD 3~~/4 interface</scene>	+	<scene name='90/904319/Inactive_tmd_interface/4'>TM3/TM4 interface</scene>

-	<scene name='90/904319/Active_helices/16'>TM6 ~~Interface~~</scene>	+	<scene name='90/904319/Active_helices/17'>TM6 interface</scene>

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Courtney Vennekotter at 14:03, 15 April 2022

Courtney Vennekotter — Fri, 15 Apr 2022 14:03:35 GMT

←Older revision		Revision as of 14:03, 15 April 2022
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	FIXED:		FIXED:
	<scene name='90/904319/Inactive_tmd_interface/3'>TMD 3/4 interface</scene>		<scene name='90/904319/Inactive_tmd_interface/3'>TMD 3/4 interface</scene>
		+
	<scene name='90/904319/Active_helices/16'>TM6 Interface</scene>		<scene name='90/904319/Active_helices/16'>TM6 Interface</scene>