Extended Data Fig. 4: Structural comparison of the ligand binding site and extracellular domains in PTH-bound PTH1R.
From: Insights into G-protein coupling preference from cryo-EM structures of Gq-bound PTH1R
a–d. Hydrophobic interactions between PTH and the ECD of PTH1R in the upright (a, c) and tilted (b, d) states. e, f. Comparison of the ligand binding modes in the transmembrane ___domain of PTH1R between the upright and tilted states. Representative interacting residues are shown as stick models. g, h. Atomic model and cryo-EM density maps around N-acetylglucosamine (NAG) modified on N1761.28 in the upright (g) and tilted (h) states. The contour levels are set to 6.2 and 7.3, respectively. i, j. Comparison of the upright (i) and tilted (j) states with the corresponding classes of Gs-bound PTH1R. k, l. Local-resolution cryo-EM density maps of the tilted state (k) and class 4 (Gs-bound) (l). The contour levels are set to 5.6 and 0.013, respectively.
