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- W4316037173 abstract "Arginine-vasopressin (AVP) and oxytocin (OT) are neurohypophysial hormones which share a high sequence and structure homology. These are two cyclic C-terminally amidated nonapeptides with different residues at position 3 and 8. In mammals, AVP and OT exert their multiple biological functions through a specific G protein-coupled receptor family: four receptors are identified, the V1a, V1b, V2 receptors (V1aR, V1bR and V2R) and the OT receptor (OTR). The chemical structure of AVP and OT was elucidated in the early 1950s. Thanks to X-ray crystallography and cryo-electron microscopy, it took however 70 additional years to determine the three-dimensional structures of the OTR and the V2R in complex with their natural agonist ligands and with different signaling partners, G proteins and β-arrestins. Today, the comparison of the different AVP/OT receptor structures gives structural insights into their orthosteric ligand binding pocket, their molecular mechanisms of activation, and their interfaces with canonical Gs, Gq and β-arrestin proteins. It also paves the way to future rational drug design and therapeutic compound development. Indeed, agonist, antagonist, biased agonist, or pharmacological chaperone analogues of AVP and OT are promising candidates to regulate different physiological functions and treat several pathologies." @default.
- W4316037173 created "2023-01-14" @default.
- W4316037173 creator A5028794237 @default.
- W4316037173 creator A5030147891 @default.
- W4316037173 creator A5054725044 @default.
- W4316037173 creator A5055040072 @default.
- W4316037173 creator A5091408597 @default.
- W4316037173 creator A5091505445 @default.
- W4316037173 date "2023-01-01" @default.
- W4316037173 modified "2023-09-27" @default.
- W4316037173 title "Structures of the arginine-vasopressin and oxytocin receptor signaling complexes" @default.
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