Sandbox Reserved 1700: Difference between revisions

The MRGPRX2 receptor structure was determined by cryo-electron microscopy (cryo-EM) <ref name= "Cao" /> <ref name= "Yang" />. Despite MRGPRX2’s novel characteristics, these structures still confirmed MRGPRX2 classification as an A-family GPCR. MRGPRX2 therefore shares the same general structural domains of all GPCR’s. This includes a <scene name='90/904305/Structure_overview_red/3'>transmembrane domain</scene> that interacts with a heterotrimeric <scene name='90/904305/Structure_overview_gprotein/2'>G-protein</scene> domain, 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. The G-protein serves as the intracellular relay for ligand binding to the receptor. In preparing the protein sample, MRGPRX2 was prepared with an <scene name='90/904305/Antibody_representation/1'>antibody scFv16</scene> in order to stabilize the transmembrane domain for proper imaging. For simplicity and to focus on the MRGPRX2 receptor, the antibody has been removed in structural scenes.