Structural basis for the activation and ligand recognition of the human oxytocin receptor
Here, Waltenspühl et al. report the cryo-EM structure of active human oxytocin receptor in complex with oxytocin and with a heterotrimeric G protein, providing insights into this hormone system critically involved in the
The small cyclic neuropeptide hormone oxytocin (OT) and its cognate receptor play a central role in the regulation of social behaviour and sexual reproduction. The human oxytocin receptor (OTR), a G protein-coupled receptor, is a key component of this system. Recent studies have highlighted the importance of oxytocin in modulating social behaviour, stress response, and reproductive processes. Understanding the molecular mechanisms underlying oxytocin's action is crucial for elucidating its physiological functions and potential therapeutic applications. Here, Waltenspühl et al. report the single-particle cryo-electron microscopy structure of the active oxytocin receptor (OTR) in complex with its cognate ligand oxytocin. This structural information provides valuable insights into the OT binding mode, the OTR activation mechanism, and the subtype specificity within the oxytocin/vasopressin receptor family. The authors' findings contribute significantly to our understanding of this hormone system and its role in regulating social behaviour and reproduction. However, it is essential to note that these results are based on a research-use-only laboratory peptide supplier's standard protocols and may not be directly applicable to clinical or therapeutic settings without further validation.