+
Open data
-
Basic information
Entry | Database: PDB / ID: 9.0E+82 | |||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | ACKR3 phosphorylated by GRK5 in complex with arrestin2 and Fab7 | |||||||||||||||||||||||||||||||||||||||
![]() |
| |||||||||||||||||||||||||||||||||||||||
![]() | SIGNALING PROTEIN/IMMUNE SYSTEM / complex / GPCR / arrestin / signaling / SIGNALING PROTEIN-IMMUNE SYSTEM complex | |||||||||||||||||||||||||||||||||||||||
Function / homology | ![]() TGFBR3 regulates TGF-beta signaling / oculomotor nerve development / MAP2K and MAPK activation / Activation of SMO / chemokine (C-X-C motif) ligand 12 signaling pathway / negative regulation of leukocyte tethering or rolling / Golgi Associated Vesicle Biogenesis / Lysosome Vesicle Biogenesis / regulation of actin polymerization or depolymerization / telencephalon cell migration ...TGFBR3 regulates TGF-beta signaling / oculomotor nerve development / MAP2K and MAPK activation / Activation of SMO / chemokine (C-X-C motif) ligand 12 signaling pathway / negative regulation of leukocyte tethering or rolling / Golgi Associated Vesicle Biogenesis / Lysosome Vesicle Biogenesis / regulation of actin polymerization or depolymerization / telencephalon cell migration / positive regulation of mesenchymal stem cell migration / C-X-C chemokine binding / chemokine receptor binding / response to ultrasound / CXCL12-activated CXCR4 signaling pathway / AP-2 adaptor complex binding / Ub-specific processing proteases / clathrin coat of coated pit / clathrin heavy chain binding / CXCR chemokine receptor binding / C-X-C chemokine receptor activity / positive regulation of axon extension involved in axon guidance / Cargo recognition for clathrin-mediated endocytosis / positive regulation of vasculature development / desensitization of G protein-coupled receptor signaling pathway / positive regulation of dopamine secretion / Signaling by ROBO receptors / induction of positive chemotaxis / Clathrin-mediated endocytosis / C-C chemokine receptor activity / integrin activation / negative regulation of dendritic cell apoptotic process / clathrin-dependent endocytosis / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage / chemokine-mediated signaling pathway / cellular response to chemokine / C-C chemokine binding / G protein-coupled receptor internalization / acetylcholine receptor binding / positive regulation of monocyte chemotaxis / inositol hexakisphosphate binding / chemokine activity / Chemokine receptors bind chemokines / blood circulation / Thrombin signalling through proteinase activated receptors (PARs) / scavenger receptor activity / G alpha (s) signalling events / clathrin binding / positive regulation of calcium ion import / small molecule binding / pseudopodium / phosphatidylinositol-3,4,5-trisphosphate binding / detection of temperature stimulus involved in sensory perception of pain / positive regulation of receptor internalization / negative regulation of Notch signaling pathway / animal organ regeneration / positive regulation of T cell migration / detection of mechanical stimulus involved in sensory perception of pain / vasculogenesis / Nuclear signaling by ERBB4 / coreceptor activity / clathrin-coated pit / positive regulation of endothelial cell proliferation / positive regulation of cell adhesion / positive regulation of neuron differentiation / axon guidance / adult locomotory behavior / cell chemotaxis / growth factor activity / G protein-coupled receptor binding / calcium-mediated signaling / defense response / recycling endosome / response to virus / receptor internalization / response to peptide hormone / intracellular calcium ion homeostasis / neuron migration / chemotaxis / integrin binding / protein transport / positive regulation of protein phosphorylation / positive regulation of cytosolic calcium ion concentration / ubiquitin-dependent protein catabolic process / cytoplasmic vesicle / : / G alpha (i) signalling events / angiogenesis / molecular adaptor activity / Estrogen-dependent gene expression / early endosome / response to hypoxia / positive regulation of ERK1 and ERK2 cascade / endosome / cell adhesion / immune response / positive regulation of cell migration / G protein-coupled receptor signaling pathway / external side of plasma membrane / signaling receptor binding Similarity search - Function | |||||||||||||||||||||||||||||||||||||||
Biological species | ![]() ![]() ![]() synthetic construct (others) | |||||||||||||||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||||||||||||||||||||||||||||||||
![]() | Chen, Q. / Fuller, J. / Tesmer, J.J.G. | |||||||||||||||||||||||||||||||||||||||
Funding support | ![]() ![]()
| |||||||||||||||||||||||||||||||||||||||
![]() | ![]() Title: ACKR3-arrestin2/3 complexes reveal molecular consequences of GRK-dependent barcoding Authors: Chen, Q. / Tesmer, J.J.G. | |||||||||||||||||||||||||||||||||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 201.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 154.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 47700MC ![]() 41288 M: map data used to model this data C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
-
Assembly
Deposited unit | ![]()
|
---|---|
1 |
|
-
Components
-Protein , 3 types, 3 molecules ABR
#1: Protein | Mass: 47055.469 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|---|
#2: Protein | Mass: 8189.663 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#5: Protein | Mass: 45356.367 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Antibody , 2 types, 2 molecules HL
#3: Antibody | Mass: 25720.758 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Production host: ![]() ![]() |
---|---|
#4: Antibody | Mass: 23471.031 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Production host: ![]() ![]() |
-Non-polymers , 1 types, 1 molecules 
#6: Chemical | ChemComp-CLR / |
---|
-Details
Has ligand of interest | N |
---|---|
Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
Component | Name: human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 Type: COMPLEX / Entity ID: #1-#5 / Source: MULTIPLE SOURCES |
---|---|
Source (natural) | Organism: ![]() ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 8 |
Specimen | Conc.: 0.7 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
-
Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 600 nm |
Image recording | Electron dose: 56 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-
Processing
EM software |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
CTF correction | Type: NONE | |||||||||
3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 104555 / Symmetry type: POINT |