Extended Data Fig. 3: Binding of ECL2 into the orthosteric pocket of GPR101.
From: Structure of GPR101–Gs enables identification of ligands with rejuvenating potential
a, EM densities of the residues of GPR101 ECL2 (orange) and its interacting residues (slate) in the orthosteric binding pocket. Three hydrophobic residues of the downstream β2-strand, L181ECL2, M184ECL2 and W186ECL2, sit in a hydrophobic groove composed of V1083.29, H1123.33, P1664.60, Y1925.38, F2005.46, Y4156.51 and I4407.39. b, The distances between the ECL2 (measured at W186 in GPR101 and the equivalent H186 in GPR52) and the traditional toggle switch residue (L6.48 in GPR101 and W6.48 GPR52). Compared with GPR52, ECL2 of GPR101 binds shallower within the orthosteric site (9.2 Å vs. 4.9 Å) and does not directly reach the toggle switch residue.
