7QVM
Human Oxytocin receptor (OTR) oxytocin Gq chimera (mGoqi) complex
Summary for 7QVM
Entry DOI | 10.2210/pdb7qvm/pdb |
EMDB information | 14180 |
Descriptor | Guanine 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 Keywords | gpcr, otr, g protein, ot, scfv16, mgoqi, oxytocin, membrane protein, signaling protein |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 6 |
Total formula weight | 140063.41 |
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 citation | Waltenspuhl, 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: 35851571DOI: 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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