Sandbox Reserved 1715: Difference between revisions

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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/7'>3 domains</scene>: the venus fly trap (VFT), cysteine rich domain (CRD), and the transmembrane domain (TMD).
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/7'>3 domains</scene>: the venus fly trap (VFT), cysteine rich domain (CRD), and the transmembrane domain (TMD).


[[Image: Orientation.png|250px|left|thumb|Figure 2. Proper orientation of mGlu about the cell membrane.]]
[[Image: Orientation_2.png|250px|left|thumb|Figure 2. Proper orientation of mGlu about the cell membrane.]]
==== Domains ====
==== 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='90/904319/Vft/1'>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='90/904320/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='90/904319/Vft/1'>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.
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