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- PDB-7ts0: Cryo-EM structure of corticotropin releasing factor receptor 2 bo... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7ts0 | ||||||||||||||||||
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Title | Cryo-EM structure of corticotropin releasing factor receptor 2 bound to Urocortin 1 and coupled with heterotrimeric Go protein | ||||||||||||||||||
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![]() | SIGNALING PROTEIN / GPCR / corticotropin releasing factor receptor 2 / Urocortin 1 / Go protein | ||||||||||||||||||
Function / homology | ![]() histone deacetylase inhibitor activity / corticotrophin-releasing factor receptor activity / corticotropin-releasing hormone receptor activity / corticotropin-releasing hormone receptor 2 binding / positive regulation of corticotropin secretion / positive regulation of behavioral fear response / negative regulation of hormone secretion / varicosity / response to auditory stimulus / drinking behavior ...histone deacetylase inhibitor activity / corticotrophin-releasing factor receptor activity / corticotropin-releasing hormone receptor activity / corticotropin-releasing hormone receptor 2 binding / positive regulation of corticotropin secretion / positive regulation of behavioral fear response / negative regulation of hormone secretion / varicosity / response to auditory stimulus / drinking behavior / positive regulation of cAMP-mediated signaling / negative regulation of appetite / positive regulation of vascular permeability / G-protein activation / Activation of the phototransduction cascade / Glucagon-type ligand receptors / Thromboxane signalling through TP receptor / Sensory perception of sweet, bitter, and umami (glutamate) taste / neuropeptide hormone activity / G beta:gamma signalling through PI3Kgamma / G beta:gamma signalling through CDC42 / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / negative regulation of cell size / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / Ca2+ pathway / G alpha (z) signalling events / G protein-coupled peptide receptor activity / Vasopressin regulates renal water homeostasis via Aquaporins / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / Adrenaline,noradrenaline inhibits insulin secretion / ADP signalling through P2Y purinoceptor 12 / G alpha (q) signalling events / Class B/2 (Secretin family receptors) / G alpha (i) signalling events / Thrombin signalling through proteinase activated receptors (PARs) / alkylglycerophosphoethanolamine phosphodiesterase activity / photoreceptor outer segment membrane / response to pain / spectrin binding / negative regulation of feeding behavior / positive regulation of calcium ion import / startle response / associative learning / peptide hormone binding / social behavior / photoreceptor outer segment / corticotropin-releasing hormone receptor 1 binding / positive regulation of collagen biosynthetic process / Synthesis, secretion, and deacylation of Ghrelin / neuropeptide signaling pathway / axon terminus / response to glucocorticoid / regulation of synaptic transmission, glutamatergic / cardiac muscle cell apoptotic process / positive regulation of cardiac muscle contraction / negative regulation of blood pressure / aerobic respiration / photoreceptor inner segment / positive regulation of DNA replication / positive regulation of translation / female pregnancy / long-term synaptic potentiation / sensory perception of sound / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / sensory perception of taste / vasodilation / heterotrimeric G-protein complex / positive regulation of interleukin-6 production / neuron projection development / signaling receptor complex adaptor activity / GTPase binding / positive regulation of peptidyl-serine phosphorylation / response to estradiol / retina development in camera-type eye / phospholipase C-activating G protein-coupled receptor signaling pathway / cell body / positive regulation of cytosolic calcium ion concentration / cellular response to hypoxia / G alpha (s) signalling events / positive regulation of cell growth / perikaryon / response to oxidative stress / cell population proliferation / negative regulation of neuron apoptotic process / cell surface receptor signaling pathway / G protein-coupled receptor signaling pathway / negative regulation of gene expression / GTPase activity / dendrite / protein-containing complex binding / positive regulation of transcription by RNA polymerase II / extracellular region / plasma membrane / cytoplasm Similarity search - Function | ||||||||||||||||||
Biological species | ![]() ![]() ![]() synthetic construct (others) | ||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.8 Å | ||||||||||||||||||
![]() | Zhao, L.-H. / Lin, J. / Mao, C. / Zhou, X.E. / Ji, S. / Shen, D. / Xiao, P. / Melcher, K. / Zhang, Y. / Yu, X. / Xu, H.E. | ||||||||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Structure insights into selective coupling of G protein subtypes by a class B G protein-coupled receptor. Authors: Li-Hua Zhao / Jingyu Lin / Su-Yu Ji / X Edward Zhou / Chunyou Mao / Dan-Dan Shen / Xinheng He / Peng Xiao / Jinpeng Sun / Karsten Melcher / Yan Zhang / Xiao Yu / H Eric Xu / ![]() ![]() Abstract: The ability to couple with multiple G protein subtypes, such as G, G, or G, by a given G protein-coupled receptor (GPCR) is critical for many physiological processes. Over the past few years, the ...The ability to couple with multiple G protein subtypes, such as G, G, or G, by a given G protein-coupled receptor (GPCR) is critical for many physiological processes. Over the past few years, the cryo-EM structures for all 15 members of the medically important class B GPCRs, all in complex with G protein, have been determined. However, no structure of class B GPCRs with G has been solved to date, limiting our understanding of the precise mechanisms of G protein coupling selectivity. Here we report the structures of corticotropin releasing factor receptor 2 (CRF2R) bound to Urocortin 1 (UCN1), coupled with different classes of heterotrimeric G proteins, G and G. We compare these structures with the structure of CRF2R in complex with G to uncover the structural differences that determine the selective coupling of G protein subtypes by CRF2R. These results provide important insights into the structural basis for the ability of CRF2R to couple with multiple G protein subtypes. | ||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 250.3 KB | Display | ![]() |
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PDB format | ![]() | 195 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 816.9 KB | Display | ![]() |
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Full document | ![]() | 821.8 KB | Display | |
Data in XML | ![]() | 34.6 KB | Display | |
Data in CIF | ![]() | 53.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 26104MC ![]() 7tryC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Protein , 4 types, 4 molecules PABG
#1: Protein | Mass: 63716.246 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#3: Protein | Mass: 40032.488 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#4: Protein | Mass: 43706.750 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#5: Protein | Mass: 7861.143 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Protein/peptide / Antibody , 2 types, 2 molecules UH
#2: Protein/peptide | Mass: 4703.277 Da / Num. of mol.: 1 / Fragment: UNP residues 83-122 / Source method: obtained synthetically / Source: (synth.) ![]() |
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#6: Antibody | Mass: 26277.299 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Production host: ![]() ![]() |
-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 |
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Sample preparation
Component | Name: Corticotropin releasing factor receptor 2 (CRF2R) bound to Urocortin 1 (UCN1) and coupled with G11 proteins Type: COMPLEX / Entity ID: all / Source: MULTIPLE SOURCES |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 7.5 |
Specimen | 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: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 4000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 64 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.13_2998: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 171435 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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