Sandbox Reserved 1723: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 44: | Line 44: | ||
=== 1. Binding Pocket === | === 1. Binding Pocket === | ||
MRGPRX2 consists of two binding pockets (seen in Figure 2). Sub-pocket 1 consists of | MRGPRX2 consists of two binding pockets (seen in Figure 2). Sub-pocket 1 consists of acidic catalytic residues Asp-184 and Glu-164 that interact with substrates by making ion pairs. There are also some hydrophobic aromatic residues, Phe-170, Trp-243, and Phe-244, towards the top of the binding pocket.<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> These residues provide stabilization with ligands through stacking. Lastly, this pocket is in close proximity with the commonly conserved disulfide bond (formed by Cys-168 and Cys-180) seen in most Class A GPCRs. The second binding pocket forms hydrophobic interactions with larger substrates (seen in Figure 2), but is generally less studied.<ref name="Cao"/> | ||
[[Image:Electro.PNG|450px|center|thumb|'''Figure 2''': Binding pocket of MRGPRX2 with cortistatin-14. Two different binding pockets are present in MRGPRX2 and cortistatin-14 interacts with both of them. <ref name="Cao"/>]] | [[Image:Electro.PNG|450px|center|thumb|'''Figure 2''': Binding pocket of MRGPRX2 with cortistatin-14. Two different binding pockets are present in MRGPRX2 and cortistatin-14 interacts with both of them. <ref name="Cao"/>]] | ||