Extended Data Fig. 5: Structure comparisons of the active state and inactive state of PTH1R induced by different ligands. | Nature

Extended Data Fig. 5: Structure comparisons of the active state and inactive state of PTH1R induced by different ligands.

From: Conserved class B GPCR activation by a biased intracellular agonist

Extended Data Fig. 5: Structure comparisons of the active state and inactive state of PTH1R induced by different ligands.The alternative text for this image may have been generated using AI.

(a–d) Structure comparisons are between the active state complexes with PTH and with PCO371. Superimposition of PTH1R from PDB: 8HA0 (PTH1R: royal blue, PTH: light coral) and the PCO371-bound PTH1R structure (PTH1R: light sea green, PCO371: crimson) reveals different peptide- and PCO371-binding sites. (a–b) Side view of different binding pockets and conformational changes in receptors; (c) Extracellular view and (d) intracellular view of PTH1R conformational changes. (e–h) Superimposed structures of PCO371-bound PTH1R in the active state, and ePTH-bound PTH1R in the inactive state from PDB: 6FJ3 (PTH1R: dark gray, ePTH: dark khaki) and the PCO371-bound PTH1R structure (PTH1R: light sea green, PCO371: crimson). (e–f) Side view of different binding pockets and conformational changes in receptors; (g) Extracellular view and (h) intracellular view of PTH1R conformational changes.

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