Sandbox Reserved 1719: Difference between revisions
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In contrast, '''Figure 6''' shows MRGPRX2 containing an <scene name='90/904324/Erc_motif/3'>ERC motif</scene> in place of the E/DRY motif, which replaces Tyr174 with Cys128.<ref name="Can"/> This replacement alters the spatial organization of the helices due to the replacement of the larger Tyr residue with the smaller Cys residue, thereby condensing the helices.<ref name="Can"/> The condensed spatial organization in MRGPRX2 accounts for the less significant conformational change observed once a ligand binds to the receptor.<ref name="Can"/> | In contrast, '''Figure 6''' shows MRGPRX2 containing an <scene name='90/904324/Erc_motif/3'>ERC motif</scene> in place of the E/DRY motif, which replaces Tyr174 with Cys128.<ref name="Can"/> This replacement alters the spatial organization of the helices due to the replacement of the larger Tyr residue with the smaller Cys residue, thereby condensing the helices.<ref name="Can"/> The condensed spatial organization in MRGPRX2 accounts for the less significant conformational change observed once a ligand binds to the receptor.<ref name="Can"/> | ||
[[Image:Disulfide_bond_comparison.png|500px|left|thumb|'''Figure 7.''' Comparison of disulfide bond location in MRGPRX2 (blue) and 5HT2AR (purple).]] | |||
=== Disulfide bonds === | === Disulfide bonds === | ||
In general, class A GPCRs have a <scene name='90/904324/5ht2a/4'>conserved disulfide bond</scene> between TM3 and ECL2.<ref name="Can"/> In contrast, '''Figure 7''' shows the location of the MRGPRX2 <scene name='90/904324/Mrgprx2_disulfide_bonds/5'>disulfide bond</scene> between Cys168 of TM4 and Cys180 of TM5, which structurally flips ECL2 to the top of TM4 and TM5.<ref name="Can"/> This creates the wide ligand-binding surface of MRGPRX2 that contributes to surface level binding and allows diverse ligand interactions.<ref name="Can"/> | In general, class A GPCRs have a <scene name='90/904324/5ht2a/4'>conserved disulfide bond</scene> between TM3 and ECL2.<ref name="Can"/> In contrast, '''Figure 7''' shows the location of the MRGPRX2 <scene name='90/904324/Mrgprx2_disulfide_bonds/5'>disulfide bond</scene> between Cys168 of TM4 and Cys180 of TM5, which structurally flips ECL2 to the top of TM4 and TM5.<ref name="Can"/> This creates the wide ligand-binding surface of MRGPRX2 that contributes to surface level binding and allows diverse ligand interactions.<ref name="Can"/> | ||
=== Sodium binding site === | === Sodium binding site === | ||
