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=== G-Protein ===

[https://proteopedia.org/wiki/index.php/G_protein GTP-binding proteins], also known as G-proteins, are heterotrimeric complexes consisting of <scene name='90/904305/Structure_overview_alpha/2'>alpha</scene>, <scene name='90/904305/Structure_overview_beta/2'>beta</scene>, and <scene name='90/904305/Structure_overview_gamma/2'>gamma</scene> subunits that interact with the intracellular transmembrane region at an <scene name='90/904306/Interface_2/2'>interface</scene> ('''Figure 2b'''). G-proteins are responsible for [https://en.wikipedia.org/wiki/Signal_transduction transmitting] extracellular signals into the cell upon activation. Activation leads to a substitution of GDP with GTP within the alpha subunit, causing the alpha subunit to disassociate from the beta and gamma subunits to initiate an intracellular signaling cascade. There are different families of G-alpha subunits, Gαi, Gαs, Gα12/13, and Gαq <ref name="Kamato">PMID: 26664886</ref>. MRGPRX2 binds to both Gαi and Gαq subunits with nearly identical structures despite slightly different amino acids present ('''Figure 2a''') <ref name= "Cao" /> <ref name= "Yang" />. Throughout this page, MGPRX2 is always shown with Gq. The major difference between the Gq and Gi bound structures comes from one amino acid difference (valine on Gq versus phenylalanine on Gi) that pushes the Gi subunit 2Å away from the arginine residue on helix 6 of the transmembrane protein. The G-protein binding GTP is a characteristic of all GPCRs regardless of any structural anomalies in the transmembrane domain.

[https://proteopedia.org/wiki/index.php/G_protein GTP-binding proteins], also known as G-proteins, are heterotrimeric complexes consisting of <scene name='90/904305/Structure_overview_alpha/2'>alpha</scene>, <scene name='90/904305/Structure_overview_beta/2'>beta</scene>, and <scene name='90/904305/Structure_overview_gamma/2'>gamma</scene> subunits that interact with the intracellular transmembrane region at an <scene name='90/904306/Interface_2/4'>interface</scene> ('''Figure 2b'''). G-proteins are responsible for [https://en.wikipedia.org/wiki/Signal_transduction transmitting] extracellular signals into the cell upon activation. Activation leads to a substitution of GDP with GTP within the alpha subunit, causing the alpha subunit to disassociate from the beta and gamma subunits to initiate an intracellular signaling cascade. There are different families of G-alpha subunits, Gαi, Gαs, Gα12/13, and Gαq <ref name="Kamato">PMID: 26664886</ref>. MRGPRX2 binds to both Gαi and Gαq subunits with nearly identical structures despite slightly different amino acids present ('''Figure 2a''') <ref name= "Cao" /> <ref name= "Yang" />. Throughout this page, MGPRX2 is always shown with Gq. The major difference between the Gq and Gi bound structures comes from one amino acid difference (valine on Gq versus phenylalanine on Gi) that pushes the Gi subunit 2Å away from the arginine residue on helix 6 of the transmembrane protein. The G-protein binding GTP is a characteristic of all GPCRs regardless of any structural anomalies in the transmembrane domain.

[[Image:Gq and gi overlay.png|500px|center|thumb|'''Figure 2a.''' Overlay of MGPRX2-Gq (red-dark blue) and MGPRX2-Gi (cyan-yellow). '''Figure 2b.''' Important residues involved in the interface between MGPRX2 and Gq/ Gi subunits. Arrow pointing to the major difference between the interfaces, which comes from the final C-terminus residue on the G-alpha subunit. In Gq, there is a valine while in Gi, there is a phenylalanine. This pushes the Gi subunit 2Å away from the arginine residue on helix 6 of the transmembrane protein. All other interactions are nearly identical. PDBs: (MRGPRX2-Gq):7s8l and (MRGPRX2-Gi):7s8m]]

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 === G-Protein ===
-[https://proteopedia.org/wiki/index.php/G_protein GTP-binding proteins], also known as G-proteins, are heterotrimeric complexes consisting of <scene name='90/904305/Structure_overview_alpha/2'>alpha</scene>, <scene name='90/904305/Structure_overview_beta/2'>beta</scene>, and <scene name='90/904305/Structure_overview_gamma/2'>gamma</scene> subunits that interact with the intracellular transmembrane region at an <scene name='90/904306/Interface_2/2'>interface</scene> ('''Figure 2b'''). G-proteins are responsible for [https://en.wikipedia.org/wiki/Signal_transduction transmitting] extracellular signals into the cell upon activation. Activation leads to a substitution of GDP with GTP within the alpha subunit, causing the alpha subunit to disassociate from the beta and gamma subunits to initiate an intracellular signaling cascade.  There are different families of G-alpha subunits, Gαi, Gαs, Gα12/13, and Gαq <ref name="Kamato">PMID: 26664886</ref>. MRGPRX2 binds to both Gαi and Gαq subunits with nearly identical structures despite slightly different amino acids present ('''Figure 2a''') <ref name= "Cao" /> <ref name= "Yang" />. Throughout this page, MGPRX2 is always shown with Gq. The major difference between the Gq and Gi bound structures comes from one amino acid difference (valine on Gq versus phenylalanine on Gi) that pushes the Gi subunit 2Å away from the arginine residue on helix 6 of the transmembrane protein. The G-protein binding GTP is a characteristic of all GPCRs regardless of any structural anomalies in the transmembrane domain.
+[https://proteopedia.org/wiki/index.php/G_protein GTP-binding proteins], also known as G-proteins, are heterotrimeric complexes consisting of <scene name='90/904305/Structure_overview_alpha/2'>alpha</scene>, <scene name='90/904305/Structure_overview_beta/2'>beta</scene>, and <scene name='90/904305/Structure_overview_gamma/2'>gamma</scene> subunits that interact with the intracellular transmembrane region at an <scene name='90/904306/Interface_2/4'>interface</scene> ('''Figure 2b'''). G-proteins are responsible for [https://en.wikipedia.org/wiki/Signal_transduction transmitting] extracellular signals into the cell upon activation. Activation leads to a substitution of GDP with GTP within the alpha subunit, causing the alpha subunit to disassociate from the beta and gamma subunits to initiate an intracellular signaling cascade.  There are different families of G-alpha subunits, Gαi, Gαs, Gα12/13, and Gαq <ref name="Kamato">PMID: 26664886</ref>. MRGPRX2 binds to both Gαi and Gαq subunits with nearly identical structures despite slightly different amino acids present ('''Figure 2a''') <ref name= "Cao" /> <ref name= "Yang" />. Throughout this page, MGPRX2 is always shown with Gq. The major difference between the Gq and Gi bound structures comes from one amino acid difference (valine on Gq versus phenylalanine on Gi) that pushes the Gi subunit 2Å away from the arginine residue on helix 6 of the transmembrane protein. The G-protein binding GTP is a characteristic of all GPCRs regardless of any structural anomalies in the transmembrane domain.
 [[Image:Gq and gi overlay.png|500px|center|thumb|'''Figure 2a.''' Overlay of MGPRX2-Gq (red-dark blue) and MGPRX2-Gi (cyan-yellow). '''Figure 2b.''' Important residues involved in the interface between MGPRX2 and Gq/ Gi subunits. Arrow pointing to the major difference between the interfaces, which comes from the final C-terminus residue on the G-alpha subunit. In Gq, there is a valine while in Gi, there is a phenylalanine. This pushes the Gi subunit 2Å away from the arginine residue on helix 6 of the transmembrane protein. All other interactions are nearly identical. PDBs: (MRGPRX2-Gq):7s8l and (MRGPRX2-Gi):7s8m]]