Sandbox Reserved 1701: Difference between revisions

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[[Image:PIF_resized.png|500px|right|thumb|'''Figure 3.''' Conserved PIF motif in 5HT2AR (teal) compared to the LLF motif found in MRGPRX2 (red). Transmembrane helices and residues are numbered and labeled to show how this structural change shifts the orientation of the helices. PDBs: (MRGPRX2): 7s8l and (5HT2A): 6wha.]]

Another motif found in most, but not all, A family GPCR’s is the PIF motif. The PIF residues (<scene name='90/904305/Llf_motif/5'>Leu-117, Leu-194, and Phe-232</scene>) are found on transmembrane helices 5, 3, and 6, respectively. In MRGPRX2, the PIF motif is changed to LLF residues. '''Figure 3''' shows the conserved PIF motif on 5HT2AR, <scene name='90/904306/Alignment_llf/1'>compared</scene> to the LLF motif on MRGPRX2. This change to LLF shifts helix 6 towards helix 3, and contributes to the tighter packing of helices <ref name="Cao">PMID: 34789874</ref> <ref name="Yang">PMID: 34789875</ref> and therefore a more surface-level ligand binding site.

Sandbox Reserved 1701: Difference between revisions

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Revision as of 01:05, 19 April 2022 view source Grace Whitacre (talk \| contribs) 181 edits No edit summary ← Older edit		Revision as of 01:06, 19 April 2022 view source Grace Whitacre (talk \| contribs) 181 edits No edit summary Newer edit →
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	[[Image:PIF_resized.png\|500px\|right\|thumb\|'''Figure 3.''' Conserved PIF motif in 5HT2AR (teal) compared to the LLF motif found in MRGPRX2 (red). Transmembrane helices and residues are numbered and labeled to show how this structural change shifts the orientation of the helices. PDBs: (MRGPRX2): 7s8l and (5HT2A): 6wha.]]		[[Image:PIF_resized.png\|500px\|right\|thumb\|'''Figure 3.''' Conserved PIF motif in 5HT2AR (teal) compared to the LLF motif found in MRGPRX2 (red). Transmembrane helices and residues are numbered and labeled to show how this structural change shifts the orientation of the helices. PDBs: (MRGPRX2): 7s8l and (5HT2A): 6wha.]]
	Another motif found in most, but not all, A family GPCR’s is the PIF motif. The PIF residues (<scene name='90/904305/Llf_motif/5'>Leu-117, Leu-194, and Phe-232</scene>) are found on transmembrane helices 5, 3, and 6, respectively. In MRGPRX2, the PIF motif is changed to LLF residues. '''Figure 3''' shows the conserved PIF motif on 5HT2AR, <scene name='90/904306/Alignment_llf/1'>compared</scene> to the LLF motif on MRGPRX2. This change to LLF shifts helix 6 towards helix 3, and contributes to the tighter packing of helices <ref name="Cao">PMID: 34789874</ref> <ref name="Yang">PMID: 34789875</ref> and therefore a more surface-level ligand binding site.		Another motif found in most, but not all, A family GPCR’s is the PIF motif. The PIF residues (<scene name='90/904305/Llf_motif/5'>Leu-117, Leu-194, and Phe-232</scene>) are found on transmembrane helices 5, 3, and 6, respectively. In MRGPRX2, the PIF motif is changed to LLF residues. '''Figure 3''' shows the conserved PIF motif on 5HT2AR, <scene name='90/904306/Alignment_llf/1'>compared</scene> to the LLF motif on MRGPRX2. This change to LLF shifts helix 6 towards helix 3, and contributes to the tighter packing of helices <ref name="Cao">PMID: 34789874</ref> <ref name="Yang">PMID: 34789875</ref> and therefore a more surface-level ligand binding site.