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7QVM

Human Oxytocin receptor (OTR) oxytocin Gq chimera (mGoqi) complex

Summary for 7QVM
Entry DOI10.2210/pdb7qvm/pdb
EMDB information14180
DescriptorGuanine nucleotide-binding protein G(o) subunit alpha,cDNA FLJ31446 fis, clone NT2NE2000909, highly similar to Guanine nucleotide-binding protein G(o) subunit alpha 1, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, ... (6 entities in total)
Functional Keywordsgpcr, otr, g protein, ot, scfv16, mgoqi, oxytocin, membrane protein, signaling protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains6
Total formula weight140063.41
Authors
Waltenspuhl, Y.,Ehrenmann, J.,Vacca, S.,Thom, C.,Medalia, O.,Pluckthun, A. (deposition date: 2022-01-21, release date: 2022-08-10, Last modification date: 2024-10-23)
Primary citationWaltenspuhl, Y.,Ehrenmann, J.,Vacca, S.,Thom, C.,Medalia, O.,Pluckthun, A.
Structural basis for the activation and ligand recognition of the human oxytocin receptor.
Nat Commun, 13:4153-4153, 2022
Cited by
PubMed 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.
PubMed: 35851571
DOI: 10.1038/s41467-022-31325-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.25 Å)
Structure validation

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