Sandbox Reserved 1723: Difference between revisions

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===== Cation =====

<scene name='90/904328/Zinc/2'>(R)-Zinc-3573</scene> is a cation ligand that selectively binds to MRGPRX2. Its N-dimethyl is inserted into subpocket 1 of the binding cavity with aromatic amino acid residues Phe-170, Trp-243, and Phe-244. In this <scene name='90/904328/Zizwithaa/3'>cavity</scene>, N-dimethyl group on the ligand makes ion pairs with Asp-184 and Glu-164. The ligand is then stabilized by stacking its ring with Trp-248 and the Cys-168 to Cys-180 disulfide bond <ref name="Yang">Yang, Fan, et al. "Structure, function and pharmacology of human itch receptor complexes." Nature, Nature Publishing Group, 17 November 2021, https://www.nature.com/articles/s41586-021-04077-y</ref>.

<scene name='90/904328/Zinc/3'>(R)-Zinc-3573</scene> is a cation ligand that selectively binds to MRGPRX2. Its N-dimethyl is inserted into subpocket 1 of the binding cavity with aromatic amino acid residues Phe-170, Trp-243, and Phe-244. In this <scene name='90/904328/Zizwithaa/3'>cavity</scene>, N-dimethyl group on the ligand makes ion pairs with Asp-184 and Glu-164. The ligand is then stabilized by stacking its ring with Trp-248 and the Cys-168 to Cys-180 disulfide bond <ref name="Yang">Yang, Fan, et al. "Structure, function and pharmacology of human itch receptor complexes." Nature, Nature Publishing Group, 17 November 2021, https://www.nature.com/articles/s41586-021-04077-y</ref>.

===== Peptide =====

<scene name='90/904328/Overview_x2_c_pt_3/3'>Cortistatin-14</scene> is one of the peptide ligands that binds to MRGPRX2. Cortistatin-14 interacts with the binding pocket through an <scene name='90/904328/Zic14_pt_3/3'>electrostatic</scene> interaction in sub-pocket 1 between Lys-3 on the peptide and Glu-164 and Asp-184 on MRGPRX2 <ref name="Cao"/>. Additionally, there are hydrophobic interactions in sub-pocket 2 between the peptide and the binding pocket due to the large hydrophobic amino acids on Cortistatin-14.

<scene name='90/904328/Overview_x2_c_pt_3/4'>Cortistatin-14</scene> is one of the peptide ligands that binds to MRGPRX2. Cortistatin-14 interacts with the binding pocket through an <scene name='90/904328/Zic14_pt_3/4'>electrostatic</scene> interaction in sub-pocket 1 between Lys-3 on the peptide and Glu-164 and Asp-184 on MRGPRX2 <ref name="Cao"/>. Additionally, there are hydrophobic interactions in sub-pocket 2 between the peptide and the binding pocket due to the large hydrophobic amino acids on Cortistatin-14.

[[Image:Newzinc.PNG |150px|center|thumb|'''Figure 3''': Structure of R-Zinc 3573. A cationic ligand selected for binding to MRGPRX2. This ligand was used as a probe for MRGPRX2 function and stabilization for structure determination. <ref name="Yang">Yang, Fan, et al. "Structure, function and pharmacology of human itch receptor complexes." Nature, Nature Publishing Group, 17 November 2021, https://www.nature.com/articles/s41586-021-04077-y</ref>]][[Image: Peptide.PNG|250px|center|thumb|'''Figure 4''': Structure of Cortistatin-14 with resolved amino acids highlighted in green.<ref name="Yang">Yang, Fan, et al. "Structure, function and pharmacology of human itch receptor complexes." Nature, Nature Publishing Group, 17 November 2021, https://www.nature.com/articles/s41586-021-04077-y</ref>]]

Sandbox Reserved 1723: Difference between revisions

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@@ Line 49: / Line 49: @@
 ===== Cation =====
-<scene name='90/904328/Zinc/2'>(R)-Zinc-3573</scene> is a cation ligand that selectively binds to MRGPRX2. Its N-dimethyl is inserted into subpocket 1 of the binding cavity with aromatic amino acid residues Phe-170, Trp-243, and Phe-244. In this <scene name='90/904328/Zizwithaa/3'>cavity</scene>, N-dimethyl group on the ligand makes ion pairs with Asp-184 and Glu-164. The ligand is then stabilized by stacking its ring with Trp-248 and the Cys-168 to Cys-180 disulfide bond <ref name="Yang">Yang, Fan, et al. "Structure, function and pharmacology of human itch receptor complexes." Nature, Nature Publishing Group, 17 November 2021, https://www.nature.com/articles/s41586-021-04077-y</ref>.
+<scene name='90/904328/Zinc/3'>(R)-Zinc-3573</scene> is a cation ligand that selectively binds to MRGPRX2. Its N-dimethyl is inserted into subpocket 1 of the binding cavity with aromatic amino acid residues Phe-170, Trp-243, and Phe-244. In this <scene name='90/904328/Zizwithaa/3'>cavity</scene>, N-dimethyl group on the ligand makes ion pairs with Asp-184 and Glu-164. The ligand is then stabilized by stacking its ring with Trp-248 and the Cys-168 to Cys-180 disulfide bond <ref name="Yang">Yang, Fan, et al. "Structure, function and pharmacology of human itch receptor complexes." Nature, Nature Publishing Group, 17 November 2021, https://www.nature.com/articles/s41586-021-04077-y</ref>.
 ===== Peptide =====
-<scene name='90/904328/Overview_x2_c_pt_3/3'>Cortistatin-14</scene> is one of the peptide ligands that binds to MRGPRX2. Cortistatin-14 interacts with the binding pocket through an <scene name='90/904328/Zic14_pt_3/3'>electrostatic</scene> interaction in sub-pocket 1 between Lys-3 on the peptide and Glu-164 and Asp-184 on MRGPRX2 <ref name="Cao"/>. Additionally, there are hydrophobic interactions in sub-pocket 2 between the peptide and the binding pocket due to the large hydrophobic amino acids on Cortistatin-14.
+<scene name='90/904328/Overview_x2_c_pt_3/4'>Cortistatin-14</scene> is one of the peptide ligands that binds to MRGPRX2. Cortistatin-14 interacts with the binding pocket through an <scene name='90/904328/Zic14_pt_3/4'>electrostatic</scene> interaction in sub-pocket 1 between Lys-3 on the peptide and Glu-164 and Asp-184 on MRGPRX2 <ref name="Cao"/>. Additionally, there are hydrophobic interactions in sub-pocket 2 between the peptide and the binding pocket due to the large hydrophobic amino acids on Cortistatin-14.
 [[Image:Newzinc.PNG |150px|center|thumb|'''Figure 3''': Structure of R-Zinc 3573. A cationic ligand selected for binding to MRGPRX2. This ligand was used as a probe for MRGPRX2 function and stabilization for structure determination. <ref name="Yang">Yang, Fan, et al. "Structure, function and pharmacology of human itch receptor complexes." Nature, Nature Publishing Group, 17 November 2021, https://www.nature.com/articles/s41586-021-04077-y</ref>]][[Image: Peptide.PNG|250px|center|thumb|'''Figure 4''': Structure of Cortistatin-14 with resolved amino acids highlighted in green.<ref name="Yang">Yang, Fan, et al. "Structure, function and pharmacology of human itch receptor complexes." Nature, Nature Publishing Group, 17 November 2021, https://www.nature.com/articles/s41586-021-04077-y</ref>]]