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Open data
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Basic information
| Entry | Database: PDB / ID: 7aa5 | ||||||
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| Title | Human TRPV4 structure in presence of 4a-PDD | ||||||
Components | Transient receptor potential cation channel subfamily V member 4,Green fluorescent protein | ||||||
Keywords | MEMBRANE PROTEIN / Ion channel. open-conformation / agonist / 4a-PDD | ||||||
| Function / homology | Function and homology informationstretch-activated, monoatomic cation-selective, calcium channel activity / blood vessel endothelial cell delamination / regulation of response to osmotic stress / osmosensor activity / vasopressin secretion / calcium ion import into cytosol / negative regulation of brown fat cell differentiation / positive regulation of microtubule depolymerization / positive regulation of striated muscle contraction / positive regulation of macrophage inflammatory protein 1 alpha production ...stretch-activated, monoatomic cation-selective, calcium channel activity / blood vessel endothelial cell delamination / regulation of response to osmotic stress / osmosensor activity / vasopressin secretion / calcium ion import into cytosol / negative regulation of brown fat cell differentiation / positive regulation of microtubule depolymerization / positive regulation of striated muscle contraction / positive regulation of macrophage inflammatory protein 1 alpha production / hyperosmotic salinity response / positive regulation of chemokine (C-X-C motif) ligand 1 production / positive regulation of chemokine (C-C motif) ligand 5 production / cartilage development involved in endochondral bone morphogenesis / cellular hypotonic salinity response / cellular hypotonic response / cortical microtubule organization / multicellular organismal-level water homeostasis / positive regulation of vascular permeability / osmosensory signaling pathway / cell-cell junction assembly / positive regulation of monocyte chemotactic protein-1 production / calcium ion import / cell volume homeostasis / cellular response to osmotic stress / regulation of aerobic respiration / TRP channels / cortical actin cytoskeleton / diet induced thermogenesis / positive regulation of macrophage chemotaxis / microtubule polymerization / calcium ion import across plasma membrane / response to mechanical stimulus / alpha-tubulin binding / beta-tubulin binding / monoatomic cation channel activity / cytoplasmic microtubule / SH2 domain binding / protein kinase C binding / actin filament organization / bioluminescence / generation of precursor metabolites and energy / positive regulation of JNK cascade / adherens junction / filopodium / response to insulin / calcium ion transmembrane transport / positive regulation of interleukin-6 production / calcium channel activity / ruffle membrane / intracellular calcium ion homeostasis / positive regulation of inflammatory response / actin filament binding / calcium ion transport / glucose homeostasis / lamellipodium / negative regulation of neuron projection development / cellular response to heat / positive regulation of cytosolic calcium ion concentration / actin binding / growth cone / actin cytoskeleton organization / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / microtubule binding / calmodulin binding / response to hypoxia / positive regulation of ERK1 and ERK2 cascade / cilium / apical plasma membrane / focal adhesion / lipid binding / protein kinase binding / cell surface / endoplasmic reticulum / negative regulation of transcription by RNA polymerase II / ATP binding / metal ion binding / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
| Biological species | Homo sapiens (human)![]() | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.18 Å | ||||||
Authors | Botte, M. / Ulrich, A.K.G. / Adaixo, R. / Gnutt, D. / Brockmann, A. / Bucher, D. / Chami, M. / Bocquet, M. / Ebbinghaus-Kintscher, U. / Puetter, V. ...Botte, M. / Ulrich, A.K.G. / Adaixo, R. / Gnutt, D. / Brockmann, A. / Bucher, D. / Chami, M. / Bocquet, M. / Ebbinghaus-Kintscher, U. / Puetter, V. / Becker, A. / Egner, U. / Stahlberg, H. / Hennig, M. / Holton, S.J. | ||||||
Citation | Journal: To Be PublishedTitle: Cryo-EM structural studies of the agonist complexed human TRPV4 ion-channel reveals novel structural rearrangements resulting in an open-conformation Authors: Botte, M. / Ulrich, A.K.G. / Adaixo, R. / Gnutt, D. / Brockmann, A. / Bucher, D. / Chami, M. / Bocquet, M. / Ebbinghaus-Kintscher, U. / Puetter, V. / Becker, A. / Egner, U. / Stahlberg, H. / ...Authors: Botte, M. / Ulrich, A.K.G. / Adaixo, R. / Gnutt, D. / Brockmann, A. / Bucher, D. / Chami, M. / Bocquet, M. / Ebbinghaus-Kintscher, U. / Puetter, V. / Becker, A. / Egner, U. / Stahlberg, H. / Hennig, M. / Holton, S.J. | ||||||
| History |
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Structure visualization
| Movie |
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7aa5.cif.gz | 462.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7aa5.ent.gz | 361.2 KB | Display | PDB format |
| PDBx/mmJSON format | 7aa5.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7aa5_validation.pdf.gz | 934.9 KB | Display | wwPDB validaton report |
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| Full document | 7aa5_full_validation.pdf.gz | 1002.3 KB | Display | |
| Data in XML | 7aa5_validation.xml.gz | 76.8 KB | Display | |
| Data in CIF | 7aa5_validation.cif.gz | 111.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/aa/7aa5 ftp://data.pdbj.org/pub/pdb/validation_reports/aa/7aa5 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 11690MC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
| #1: Protein | Mass: 106241.820 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human), (gene. exp.) ![]() Gene: TRPV4, VRL2, VROAC, GFP / Production host: Baculovirus expression vector pFastBac1-HM / References: UniProt: Q9HBA0, UniProt: P42212#2: Chemical | ChemComp-CA / | 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: Human TRPV4 in complex with 4a-PDD / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT | ||||||||||||
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| Molecular weight | Experimental value: NO | ||||||||||||
| Source (natural) |
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| Source (recombinant) | Organism: Baculovirus expression vector pFastBac1-HM | ||||||||||||
| Buffer solution | pH: 8 | ||||||||||||
| Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 | ||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 90 % / Chamber temperature: 283 K / Details: blot for 3 seconds before plunging |
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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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 50 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 4.18 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 51215 / Symmetry type: POINT |
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Homo sapiens (human)

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UCSF Chimera








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Baculovirus expression vector pFastBac1-HM

