Structural basis for the activation and ligand recognition of the human oxytocin receptor
Copyright policy )Structural basis for the activation and ligand recognition of the human oxytocin receptor
Abstract The small cyclic neuropeptide hormone oxytocin (OT) and its cognate receptor play a central role in the regulation of social behaviour and sexual reproduction. Here we report the single-particle cryo-electron microscopy structure of the active oxytocin receptor (OTR) in complex with its cognate ligand oxytocin. Our structure provides high-resolution insights into the OT binding mode, the OTR activation mechanism as well as the subtype specificity within the oxytocin/vasopressin receptor family.
- University of Zurich Switzerland
- Novo Nordisk (Switzerland) Switzerland
- University of Zurich
- UNIVERSITAET ZUERICH Switzerland
- Univerisity of Zurich Finland
1000 Multidisciplinary, Receptors, Vasopressin, Science, Q, Cryoelectron Microscopy, 610 Medicine & health, 1600 General Chemistry, Ligands, Oxytocin, 3100 General Physics and Astronomy, Article, Structure-Activity Relationship, 1300 General Biochemistry, Genetics and Molecular Biology, Receptors, Oxytocin, 10019 Department of Biochemistry, 570 Life sciences; biology, Humans, Protein Structural Elements
1000 Multidisciplinary, Receptors, Vasopressin, Science, Q, Cryoelectron Microscopy, 610 Medicine & health, 1600 General Chemistry, Ligands, Oxytocin, 3100 General Physics and Astronomy, Article, Structure-Activity Relationship, 1300 General Biochemistry, Genetics and Molecular Biology, Receptors, Oxytocin, 10019 Department of Biochemistry, 570 Life sciences; biology, Humans, Protein Structural Elements
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