Fig. 3: Selectivity mechanism of PGF2α and PGE2 towards the FP receptor and EP3 receptor. | Nature Communications

Fig. 3: Selectivity mechanism of PGF2α and PGE2 towards the FP receptor and EP3 receptor.

From: Structures of human prostaglandin F2α receptor reveal the mechanism of ligand and G protein selectivity

Fig. 3

a H812.54 forms a hydrogen bond with 11-hydroxyl on the F-ring of carboprost (orange sticks) in the FP receptor (blue). The 9-hydroxyl interacts with S331.39 in the FP receptor in a space created by the small side chain of G852.58. b In the EP3 receptor (green), Q1032.54 replaces H812.54 of the FP receptor and does not form a hydrogen bond with 11-hydroxyl of PGE2 (red sticks). The 9-carbonyl of PGE2 interacts with T1072.58. S331.39 of the FP receptor is replaced by P551.39 in the EP3 receptor. c The PGF2α activation profile of FP receptor and mutants revealed by NanoBiT assay. d The PGE2 activation profile of FP receptor and mutants revealed by NanoBiT assay. e The PGF2α activation profile of EP3 receptor and mutants revealed by NanoBiT assay. f The PGE2 activation profile of EP3 receptor and mutants revealed by NanoBiT assay. Values represent the means ± SD of 3 independent experiments. Source data are provided as a Source Data file.

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