+
Open data
-
Basic information
| Entry | Database: PDB / ID: 7x10 | ||||||
|---|---|---|---|---|---|---|---|
| Title | ADGRL3/miniG12 complex | ||||||
Components |
| ||||||
Keywords | MEMBRANE PROTEIN / GPCR | ||||||
| Function / homology | Function and homology informationlocomotion involved in locomotory behavior / Rho-activating G protein-coupled receptor signaling pathway / cell adhesion mediator activity / excitatory synapse assembly / : / maintenance of postsynaptic specialization structure / positive regulation of synapse assembly / synapse assembly / response to cocaine / molecular condensate scaffold activity ...locomotion involved in locomotory behavior / Rho-activating G protein-coupled receptor signaling pathway / cell adhesion mediator activity / excitatory synapse assembly / : / maintenance of postsynaptic specialization structure / positive regulation of synapse assembly / synapse assembly / response to cocaine / molecular condensate scaffold activity / G protein-coupled receptor activity / synapse organization / Schaffer collateral - CA1 synapse / Olfactory Signaling Pathway / Activation of the phototransduction cascade / adenylate cyclase-activating G protein-coupled receptor signaling pathway / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / neuron migration / 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 / cell-cell junction / 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 / carbohydrate binding / GTPase binding / Ca2+ pathway / fibroblast proliferation / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / G alpha (i) signalling events / G alpha (s) signalling events / phospholipase C-activating G protein-coupled receptor signaling pathway / G alpha (q) signalling events / Ras protein signal transduction / postsynaptic membrane / cell surface receptor signaling pathway / Extra-nuclear estrogen signaling / cell population proliferation / G protein-coupled receptor signaling pathway / axon / lysosomal membrane / GTPase activity / calcium ion binding / synapse / protein-containing complex binding / glutamatergic synapse / signal transduction / extracellular exosome / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human)![]() | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.93 Å | ||||||
Authors | He, Y. / Qian, Y. | ||||||
| Funding support | China, 1items
| ||||||
Citation | Journal: Mol Cell / Year: 2022Title: Structural insights into adhesion GPCR ADGRL3 activation and G, G, G, and G coupling. Authors: Yu Qian / Zhengxiong Ma / Chunhong Liu / Xinzhi Li / Xinyan Zhu / Na Wang / Zhenmei Xu / Ruixue Xia / Jiale Liang / Yaning Duan / Han Yin / Yangjie Xiong / Anqi Zhang / Changyou Guo / Zheng ...Authors: Yu Qian / Zhengxiong Ma / Chunhong Liu / Xinzhi Li / Xinyan Zhu / Na Wang / Zhenmei Xu / Ruixue Xia / Jiale Liang / Yaning Duan / Han Yin / Yangjie Xiong / Anqi Zhang / Changyou Guo / Zheng Chen / Zhiwei Huang / Yuanzheng He / ![]() Abstract: Adhesion G-protein-coupled receptors (aGPCRs) play key roles in a diversity of physiologies. A hallmark of aGPCR activation is the removal of the inhibitory GAIN domain and the dipping of the cleaved ...Adhesion G-protein-coupled receptors (aGPCRs) play key roles in a diversity of physiologies. A hallmark of aGPCR activation is the removal of the inhibitory GAIN domain and the dipping of the cleaved stalk peptide into the ligand-binding pocket of receptors; however, the detailed mechanism remains obscure. Here, we present cryoelectron microscopy (cryo-EM) structures of ADGRL3 in complex with G, G, G, and G. The structures reveal unique ligand-engaging mode, distinctive activation conformation, and key mechanisms of aGPCR activation. The structures also reveal the uncharted structural information of GPCR/G coupling. A comparison of G, G, G, and G engagements with ADGRL3 reveals the key determinant of G-protein coupling on the far end of αH5 of Gα. A detailed analysis of the engagements allows us to design mutations that specifically enhance one pathway over others. Taken together, our study lays the groundwork for understanding aGPCR activation and G-protein-coupling selectivity. | ||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 7x10.cif.gz | 236.2 KB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb7x10.ent.gz | 168 KB | Display | PDB format |
| PDBx/mmJSON format | 7x10.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7x10_validation.pdf.gz | 726 KB | Display | wwPDB validaton report |
|---|---|---|---|---|
| Full document | 7x10_full_validation.pdf.gz | 728.8 KB | Display | |
| Data in XML | 7x10_validation.xml.gz | 36.7 KB | Display | |
| Data in CIF | 7x10_validation.cif.gz | 57 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x1/7x10 ftp://data.pdbj.org/pub/pdb/validation_reports/x1/7x10 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 32932MC ![]() 7wy5C ![]() 7wy8C ![]() 7wybC M: map data used to model this data C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
-
Assembly
| Deposited unit | ![]()
|
|---|---|
| 1 |
|
-
Components
| #1: Protein | Mass: 39957.145 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Insect BA phytoplasma (bacteria) |
|---|---|
| #2: Protein | Mass: 37915.496 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GNB1 / Production host: Insect BA phytoplasma (bacteria) / References: UniProt: P62873 |
| #3: Antibody | Mass: 26277.299 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Insect BA phytoplasma (bacteria) |
| #4: 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: Insect BA phytoplasma (bacteria) / References: UniProt: P59768 |
| #5: Protein | Mass: 172044.625 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Insect BA phytoplasma (bacteria) / References: UniProt: Q80TS3 |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
|---|---|
| EM experiment | Aggregation state: 3D ARRAY / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
| Component | Name: GPCR/G-protein complex / Type: COMPLEX / Entity ID: all / Source: MULTIPLE SOURCES |
|---|---|
| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Insect BA phytoplasma (bacteria) |
| Buffer solution | pH: 7.5 |
| 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 |
|---|---|
| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2300 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
| EM diffraction | Camera length: 800 mm |
| EM diffraction shell | Resolution: 3→5.5 Å / Fourier space coverage: 93.2 % / Multiplicity: 2.5 / Num. of structure factors: 244 / Phase residual: 13.5 ° |
| EM diffraction stats | Fourier space coverage: 90.3 % / High resolution: 2.83 Å / Num. of intensities measured: 1590 / Num. of structure factors: 325 / Phase error rejection criteria: 20 / Rmerge: 0.198 |
-
Processing
| EM software |
| |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| CTF correction | Type: NONE | |||||||||
| 3D reconstruction | Resolution: 2.93 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 320000 / Symmetry type: POINT | |||||||||
| Atomic model building | Protocol: OTHER / Space: REAL | |||||||||
| Atomic model building | PDB-ID: 6VMS Pdb chain-ID: A / Accession code: 6VMS / Source name: PDB / Type: experimental model |
Movie
Controller
About Yorodumi




Homo sapiens (human)

China, 1items
Citation






PDBj



















gel filtration
Insect BA phytoplasma (bacteria)

