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Yorodumi- PDB-7qvm: Human Oxytocin receptor (OTR) oxytocin Gq chimera (mGoqi) complex -
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-Basic information
Entry | Database: PDB / ID: 7qvm | ||||||
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Title | Human Oxytocin receptor (OTR) oxytocin Gq chimera (mGoqi) complex | ||||||
Components |
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Keywords | SIGNALING PROTEIN / GPCR / OTR / G protein / OT / scFv16 / mGoqi / oxytocin / membrane protein | ||||||
Function / homology | Function and homology information oxytocin receptor activity / response to anoxia / oxytocin receptor binding / neurohypophyseal hormone activity / V1A vasopressin receptor binding / guanyl nucleotide binding / Vasopressin-like receptors / regulation of systemic arterial blood pressure by vasopressin / vasopressin receptor activity / maternal process involved in parturition ...oxytocin receptor activity / response to anoxia / oxytocin receptor binding / neurohypophyseal hormone activity / V1A vasopressin receptor binding / guanyl nucleotide binding / Vasopressin-like receptors / regulation of systemic arterial blood pressure by vasopressin / vasopressin receptor activity / maternal process involved in parturition / positive regulation of penile erection / positive regulation of uterine smooth muscle contraction / positive regulation of norepinephrine secretion / sperm ejaculation / telencephalon development / mu-type opioid receptor binding / corticotropin-releasing hormone receptor 1 binding / maternal behavior / positive regulation of blood pressure / neuropeptide hormone activity / digestive tract development / positive regulation of synapse assembly / dopamine receptor signaling pathway / eating behavior / suckling behavior / social behavior / microvillus / peptide hormone binding / estrous cycle / G protein-coupled serotonin receptor binding / positive regulation of vasoconstriction / cellular response to hormone stimulus / ERK1 and ERK2 cascade / response to amphetamine / lactation / positive regulation of synaptic transmission, glutamatergic / response to cocaine / response to progesterone / muscle contraction / secretory granule / response to cytokine / female pregnancy / positive regulation of synaptic transmission, GABAergic / adherens junction / peptide binding / G-protein beta/gamma-subunit complex binding / Olfactory Signaling Pathway / Activation of the phototransduction cascade / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / G-protein activation / G protein-coupled acetylcholine receptor signaling pathway / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / Prostacyclin signalling through prostacyclin receptor / Glucagon signaling in metabolic regulation / G beta:gamma signalling through CDC42 / ADP signalling through P2Y purinoceptor 12 / G beta:gamma signalling through BTK / Sensory perception of sweet, bitter, and umami (glutamate) taste / memory / response to peptide hormone / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / photoreceptor disc membrane / Adrenaline,noradrenaline inhibits insulin secretion / Glucagon-type ligand receptors / Vasopressin regulates renal water homeostasis via Aquaporins / G alpha (z) signalling events / cellular response to catecholamine stimulus / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / ADORA2B mediated anti-inflammatory cytokines production / adenylate cyclase-activating dopamine receptor signaling pathway / ADP signalling through P2Y purinoceptor 1 / G beta:gamma signalling through PI3Kgamma / cellular response to prostaglandin E stimulus / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / sensory perception of taste / GPER1 signaling / G-protein beta-subunit binding / heterotrimeric G-protein complex / Inactivation, recovery and regulation of the phototransduction cascade / extracellular vesicle / G alpha (12/13) signalling events / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / response to estradiol / retina development in camera-type eye / GTPase binding / Ca2+ pathway / phospholipase C-activating G protein-coupled receptor signaling pathway / positive regulation of cold-induced thermogenesis / heart development / positive regulation of cytosolic calcium ion concentration / G alpha (i) signalling events / fibroblast proliferation / G alpha (s) signalling events / G alpha (q) signalling events / Ras protein signal transduction Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Mus musculus (house mouse) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.25 Å | ||||||
Authors | Waltenspuhl, Y. / Ehrenmann, J. / Vacca, S. / Thom, C. / Medalia, O. / Pluckthun, A. | ||||||
Funding support | Switzerland, 1items
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Citation | Journal: Nat Commun / Year: 2022 Title: Structural basis for the activation and ligand recognition of the human oxytocin receptor. Authors: Yann Waltenspühl / Janosch Ehrenmann / Santiago Vacca / Cristian Thom / Ohad Medalia / Andreas Plückthun / 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- ...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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7qvm.cif.gz | 200.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7qvm.ent.gz | 158.7 KB | Display | PDB format |
PDBx/mmJSON format | 7qvm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qv/7qvm ftp://data.pdbj.org/pub/pdb/validation_reports/qv/7qvm | HTTPS FTP |
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-Related structure data
Related structure data | 14180MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Guanine nucleotide-binding protein ... , 3 types, 3 molecules ABG
#1: Protein | Mass: 25650.412 Da / Num. of mol.: 1 Mutation: E9D,R10K,L13V,A18M,I344L,A345Q,N346L,G350E,C351Y,G352N,Y354V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GNAO1 / Production host: Spodoptera frugiperda (fall armyworm) References: UniProt: A0A1W2PS82, UniProt: B3KP89, UniProt: P09471 |
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#2: Protein | Mass: 39086.641 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GNB1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P62873 |
#3: Protein | Mass: 7861.143 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GNG2 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P59768 |
-Protein/peptide / Protein / Antibody , 3 types, 3 molecules LRS
#4: Protein/peptide | Mass: 1008.196 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P01178 |
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#5: Protein | Mass: 39777.293 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: OXTR / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P30559 |
#6: Antibody | Mass: 26679.721 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Spodoptera frugiperda (fall armyworm) |
-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component |
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Source (natural) |
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Source (recombinant) |
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Buffer solution | pH: 7.4 | ||||||||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: OTHER / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm |
Image recording | Electron dose: 63.78 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
EM software | Name: Gctf / Category: CTF correction |
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CTF correction | Type: NONE |
3D reconstruction | Resolution: 3.25 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 392369 / Symmetry type: POINT |