Sandbox Reserved 1719: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 100: Line 100:


=== DRY/ERC motif ===
=== DRY/ERC motif ===
The majority of class A GPCRs have a [https://proteopedia.org/wiki/index.php/A_Physical_Model_of_the_%CE%B22-Adrenergic_Receptor#conserved%20DRY%20motif conserved E/DRY motif]. However, MRGPRX2 contains an <scene name='90/904324/Erc_motif/3'>ERC motif</scene>, which replaces Tyr174 with Cys128.<ref name="Can"/> This replacement alters the spatial organization of the helices due to the fact that Tyr is no longer present to push the helices outward.<ref name="Can"/> As a result, the binding site in MRGPRX2 is shallower which lead to surface-level ligand interactions.<ref name="Can"/>
The majority of class A GPCRs have a [https://proteopedia.org/wiki/index.php/A_Physical_Model_of_the_%CE%B22-Adrenergic_Receptor#conserved%20DRY%20motif conserved E/DRY motif] that is responsible for creating salt bridges that maintain the inactive conformation of the receptor until ligand binding.<ref name="Can"/>
In contrast, '''Figure 7''' 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 change once a ligand binds to the receptor.<ref name="Can"/>
[[Image:B2AR_motif.png|500px|center|thumb|'''Figure 7.''' Comparison of ERC motif in MRGPRX2 (blue) and conserved DRY motif in β<sub>2</sub>AR (green).]]
[[Image:B2AR_motif.png|500px|center|thumb|'''Figure 7.''' Comparison of ERC motif in MRGPRX2 (blue) and conserved DRY motif in β<sub>2</sub>AR (green).]]


Retrieved from "https://proteopedia.org/Sandbox_Reserved_1719"