Sandbox Reserved 1701: Difference between revisions

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[[Image:Screen Shot 2022-03-15 at 10.23.20 AM.png|200px|left|thumb|'''Figure 4.''' ERC Motif]]

The E/DRY motif in most class A GPCRs is responsible for forming salt bridges with surrounding residues and TM6. These salt bridges maintain the inactive conformation of the receptor until ligand binding breaks the ionic "lock" from these interactions. MRGPRX2 has an <scene name='90/904306/Erc_motif_3/1'>ERC Motif</scene> rather than the typically [https://proteopedia.org/wiki/index.php/A_Physical_Model_of_the_%CE%B22-Adrenergic_Receptor#conserved%20DRY%20motif conserved E/DRY Motif]. The amino acid residue shift from TYR-174 to CYS-128 allows compaction of the helices in MRGPRX2 where the standard TYR physically pushes the TMD helices apart('''Figure 4'''). The conserved residues E and R still form salt bridges with nearby residues. This and the closer packing of the helices contribute to a less significant TMD conformational change upon ligand binding ('''Figure 10''').

Sandbox Reserved 1701: Difference between revisions

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Revision as of 14:46, 12 April 2022 view source Grace Whitacre (talk \| contribs) 181 edits No edit summary ← Older edit		Revision as of 14:47, 12 April 2022 view source Grace Whitacre (talk \| contribs) 181 edits No edit summary Newer edit →
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	[[Image:Screen Shot 2022-03-15 at 10.23.20 AM.png\|200px\|left\|thumb\|'''Figure 4.''' ERC Motif]]		[[Image:Screen Shot 2022-03-15 at 10.23.20 AM.png\|200px\|left\|thumb\|'''Figure 4.''' ERC Motif]]
	The E/DRY motif in most class A GPCRs is responsible for forming salt bridges with surrounding residues and TM6. These salt bridges maintain the inactive conformation of the receptor until ligand binding breaks the ionic "lock" from these interactions. MRGPRX2 has an <scene name='90/904306/Erc_motif_3/1'>ERC Motif</scene> rather than the typically [https://proteopedia.org/wiki/index.php/A_Physical_Model_of_the_%CE%B22-Adrenergic_Receptor#conserved%20DRY%20motif conserved E/DRY Motif]. The amino acid residue shift from TYR-174 to CYS-128 allows compaction of the helices in MRGPRX2 where the standard TYR physically pushes the TMD helices apart('''Figure 4'''). The conserved residues E and R still form salt bridges with nearby residues. This and the closer packing of the helices contribute to a less significant TMD conformational change upon ligand binding ('''Figure 10''').		The E/DRY motif in most class A GPCRs is responsible for forming salt bridges with surrounding residues and TM6. These salt bridges maintain the inactive conformation of the receptor until ligand binding breaks the ionic "lock" from these interactions. MRGPRX2 has an <scene name='90/904306/Erc_motif_3/1'>ERC Motif</scene> rather than the typically [https://proteopedia.org/wiki/index.php/A_Physical_Model_of_the_%CE%B22-Adrenergic_Receptor#conserved%20DRY%20motif conserved E/DRY Motif]. The amino acid residue shift from TYR-174 to CYS-128 allows compaction of the helices in MRGPRX2 where the standard TYR physically pushes the TMD helices apart('''Figure 4'''). The conserved residues E and R still form salt bridges with nearby residues. This and the closer packing of the helices contribute to a less significant TMD conformational change upon ligand binding ('''Figure 10''').