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Yorodumi- PDB-9k26: PrRP31 bound prolactin-releasing peptide receptor coupled with Gi... -
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Basic information
| Entry | Database: PDB / ID: 9k26 | ||||||
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| Title | PrRP31 bound prolactin-releasing peptide receptor coupled with Gi protein complex | ||||||
 Components | 
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 Keywords | PEPTIDE BINDING PROTEIN/IMMUNE SYSTEM / a peptide related GPCR-Gi complex / STRUCTURAL PROTEIN / PEPTIDE BINDING PROTEIN / PEPTIDE BINDING PROTEIN-IMMUNE SYSTEM complex | ||||||
| Function / homology |  Function and homology informationprolactin-releasing peptide receptor binding / autonomic nervous system development / neuropeptide Y receptor activity / reduction of food intake in response to dietary excess / neuropeptide receptor activity / tissue homeostasis / energy reserve metabolic process / neuropeptide hormone activity / neuropeptide binding / hormone metabolic process ...prolactin-releasing peptide receptor binding / autonomic nervous system development / neuropeptide Y receptor activity / reduction of food intake in response to dietary excess / neuropeptide receptor activity / tissue homeostasis / energy reserve metabolic process / neuropeptide hormone activity / neuropeptide binding / hormone metabolic process / feeding behavior / fat cell differentiation / regulation of multicellular organism growth / response to glucose / adenylate cyclase inhibitor activity / positive regulation of protein localization to cell cortex / Adenylate cyclase inhibitory pathway / T cell migration / D2 dopamine receptor binding / response to prostaglandin E / adenylate cyclase regulator activity / G protein-coupled serotonin receptor binding / adenylate cyclase-inhibiting serotonin receptor signaling pathway / cellular response to forskolin / regulation of mitotic spindle organization / Peptide ligand-binding receptors / Regulation of insulin secretion / positive regulation of cholesterol biosynthetic process / female pregnancy / negative regulation of insulin secretion / G protein-coupled receptor binding / G protein-coupled receptor activity / response to insulin / response to peptide hormone / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / hormone activity / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / lipid metabolic process / G-protein beta/gamma-subunit complex binding / centriolar satellite / 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 / G protein-coupled acetylcholine receptor signaling pathway / Activation of G protein gated Potassium channels / Inhibition  of voltage gated Ca2+ channels via Gbeta/gamma subunits / G-protein activation / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through CDC42 / Glucagon signaling in metabolic regulation / G beta:gamma signalling through BTK / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / ADP signalling through P2Y purinoceptor 12 / photoreceptor disc membrane / Sensory perception of sweet, bitter, and umami (glutamate) taste / Glucagon-type ligand receptors / Adrenaline,noradrenaline inhibits insulin secretion / Vasopressin regulates renal water homeostasis via Aquaporins / GDP binding / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / G alpha (z) signalling events / cellular response to catecholamine stimulus / ADP signalling through P2Y purinoceptor 1 / ADORA2B mediated anti-inflammatory cytokines production / G beta:gamma signalling through PI3Kgamma / adenylate cyclase-activating dopamine receptor signaling pathway / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / Inactivation, recovery and regulation of the phototransduction cascade / cellular response to prostaglandin E stimulus / G-protein beta-subunit binding / heterotrimeric G-protein complex / G alpha (12/13) signalling events / sensory perception of taste / extracellular vesicle / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / retina development in camera-type eye / G protein activity / GTPase binding / Ca2+ pathway / fibroblast proliferation / midbody / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / cell cortex / G alpha (i) signalling events / G alpha (s) signalling events / phospholipase C-activating G protein-coupled receptor signaling pathway / G alpha (q) signalling events / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / Ras protein signal transduction / Extra-nuclear estrogen signaling / cell population proliferation / neuron projection / cilium / ciliary basal body / G protein-coupled receptor signaling pathway / lysosomal membrane Similarity search - Function  | ||||||
| Biological species |  Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | ||||||
 Authors | Wu, Z. / Du, Y. / Chen, G. | ||||||
| Funding support | 1items 
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 Citation |  Journal: to be publishedTitle: a peptide receptor complex structure Authors: Wu, Z. / Du, Y. / Jun, X.  | ||||||
| History | 
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Structure visualization
| Structure viewer | Molecule:  Molmil Jmol/JSmol | 
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Downloads & links
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Download
| PDBx/mmCIF format |  9k26.cif.gz | 217.1 KB | Display |  PDBx/mmCIF format | 
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| PDB format |  pdb9k26.ent.gz | 167.7 KB | Display |  PDB format | 
| PDBx/mmJSON format |  9k26.json.gz | Tree view |  PDBx/mmJSON format | |
| Others |  Other downloads | 
-Validation report
| Summary document |  9k26_validation.pdf.gz | 1.4 MB | Display |  wwPDB validaton report | 
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| Full document |  9k26_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML |  9k26_validation.xml.gz | 49.7 KB | Display | |
| Data in CIF |  9k26_validation.cif.gz | 73.1 KB | Display | |
| Arichive directory |  https://data.pdbj.org/pub/pdb/validation_reports/k2/9k26 ftp://data.pdbj.org/pub/pdb/validation_reports/k2/9k26 | HTTPS FTP  | 
-Related structure data
| Related structure data | ![]() 61991MC ![]() 9k27C M: map data used to model this data C: citing same article (  | 
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| Similar structure data | Similarity search - Function & homology  F&H Search | 
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Links
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Assembly
| Deposited unit | ![]() 
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| 1 | 
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Components
-Prolactin-releasing peptide  ... , 2 types, 2 molecules AF 
| #1: Protein |   Mass: 41163.520 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Homo sapiens (human) / Gene: PRLHR, GPR10, GR3Production host:  Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)References: UniProt: P49683  | 
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| #2: Protein/peptide |   Mass: 3671.186 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.)   Homo sapiens (human) / References: UniProt: P81277 | 
-Guanine nucleotide-binding protein  ... , 3 types, 3 molecules CBG  
| #3: Protein |   Mass: 40153.672 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Homo sapiens (human) / Gene: GNAI1Production host:  Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)References: UniProt: P63096  | 
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| #4: Protein |   Mass: 39286.891 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Homo sapiens (human) / Gene: GNB1Production host:  Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)References: UniProt: P62873  | 
| #5: Protein |   Mass: 7861.143 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Homo sapiens (human) / Gene: GNG2Production host:  Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)References: UniProt: P59768  | 
-Antibody , 1 types, 1 molecules S
| #6: Antibody |   Mass: 27707.885 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Homo sapiens (human)Production host:  Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths) | 
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-Details
| Has ligand of interest | N | 
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| Has protein modification | Y | 
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY | 
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction | 
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Sample preparation
| Component | 
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| Molecular weight | Value: 0.13 MDa / Experimental value: YES | ||||||||||||||||||||||||
| Source (natural) | Organism:  Homo sapiens (human) | ||||||||||||||||||||||||
| Source (recombinant) | Organism:  Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths) | ||||||||||||||||||||||||
| Buffer solution | pH: 7.5 | ||||||||||||||||||||||||
| Specimen | Conc.: 5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE | 
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company  | 
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| Microscopy | Model: TFS KRIOS | 
| Electron gun | Electron source:  FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM | 
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1200 nm | 
| Image recording | Electron dose: 1.13 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) | 
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Processing
| EM software | 
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
| Particle selection | Num. of particles selected: 1018641 | ||||||||||||
| 3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 1018641 / Symmetry type: POINT | 
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Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
FIELD EMISSION GUN