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- PDB-6pvl: Cryo-EM structure of mouse TRPV3 in closed state at 42 degrees Celsius -
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Open data
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Basic information
Entry | Database: PDB / ID: 6pvl | ||||||
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Title | Cryo-EM structure of mouse TRPV3 in closed state at 42 degrees Celsius | ||||||
![]() | Transient receptor potential cation channel subfamily V member 3 | ||||||
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Function / homology | ![]() negative regulation of hair cycle / ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Singh, A.K. / McGoldrick, L.L. / Sobolevsky, A.I. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis of temperature sensation by the TRP channel TRPV3. Authors: Appu K Singh / Luke L McGoldrick / Lusine Demirkhanyan / Merfilius Leslie / Eleonora Zakharian / Alexander I Sobolevsky / ![]() Abstract: We present structures of mouse TRPV3 in temperature-dependent open, closed and intermediate states that suggest two-step activation of TRPV3 by heat. During the strongly temperature-dependent first ...We present structures of mouse TRPV3 in temperature-dependent open, closed and intermediate states that suggest two-step activation of TRPV3 by heat. During the strongly temperature-dependent first step, sensitization, the channel pore remains closed while S6 helices undergo α-to-π transitions. During the weakly temperature-dependent second step, channel opening, tight association of the S1-S4 and pore domains is stabilized by changes in the carboxy-terminal and linker domains. | ||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 458.2 KB | Display | ![]() |
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PDB format | ![]() | 376.8 KB | Display | ![]() |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 20492MC ![]() 6pvmC ![]() 6pvnC ![]() 6pvoC ![]() 6pvpC ![]() 6pvqC 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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Components
#1: Protein | Mass: 92630.695 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Chemical | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: ![]() |
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Sample preparation
Component | Name: TRPV3 in closed state at 42 degree Celsius![]() |
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Source (natural) | Organism: ![]() ![]() ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 8 Details: 150 mM NaCl, 20 mM Tris-HCl, pH 8.0, 1 mM BME, 0.01% GDN |
Specimen | Conc.: 4.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied![]() ![]() |
Specimen support | Grid material: GOLD |
Vitrification![]() | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 42 K |
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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![]() |
Image recording | Electron dose: 57 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
EM software | Name: RELION / Category: 3D reconstruction![]() |
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CTF correction![]() | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
Symmetry | Point symmetry![]() ![]() |
3D reconstruction![]() | Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 33741 / Num. of class averages: 1 / Symmetry type: POINT |