CBD and TRPV2
Relative of TRPV1 · ion channel.
Relative of TRPV1 · ion channel. Where this target is found in the body, lab findings on CBD, the strength of evidence and the molecular structure, with sources.
CBD's other targetsStructure: PDB 6U88Last updated:
What's on this page?
Interactive 3D · real anatomy and real data
Where in your body are the cannabinoid receptors?
About 1.4 MB to download.
Regions
How to read it Choose a region, or tap a glowing point on the map.
- Solid light is the CB1 receptor, a ring is CB2. Each region has its own color; the color only tells regions apart.
- The strength of the light is the receptor gene level measured in human tissue (Human Protein Atlas). That is why the liver’s point is dim: a healthy liver has few receptors.
- With the layer selector above you can also see other receptors, the enzymes that make and break down endocannabinoids, and the liver enzymes that break down CBD and THC.
- Every piece of information shows its source and the type of evidence (human, animal, cell). You can change the reading level above.
- Drag to rotate. Use the + and − buttons to zoom; on a computer, Ctrl or ⌘ with the scroll wheel, on a phone, two fingers.
Where is it, and what does it do?
TRPV2 is an ion channel closely related to TRPV1. It does not respond to capsaicin or moderate heat; it opens at a high threshold of about 52 °C. It stands out in medium- and large-diameter nerve cells of the sensory ganglia, but it is not found only in the nervous system. Caterina 1999Cell / labAnimal
Findings on CBD
In cell experiments, CBD was the strongest activator of this channel among the cannabinoids tested: half of the effect was seen at 3.7 µM (14 µM for THC). The structure in which CBD has been imaged bound to one of its targets is also here: cryo-electron microscopy solved the CBD-bound structure of rat TRPV2 and showed CBD sitting in a fat-loving pocket between neighboring subunits. Qin 2008Cell / labAnimalPumroy 2019Molecular structure (lab)Gochman 2023Molecular structure (lab)Cell / lab
Student level: experiments and numbers
Qin 2008: CBD was the most potent and most efficacious TRPV2 agonist (EC50 3.7 µM), followed by Δ⁹-THC (14 µM) and cannabinol (77.7 µM); in cultured rat dorsal root ganglion neurons, it triggered CGRP release independently of cannabinoid receptors and TRPV1, and siRNA showed that at least part of the release was TRPV2-mediated. Pumroy 2019: full-length rat TRPV2 in nanodiscs, with and without CBD; CBD sits in a hydrophobic pocket between the S5 and S6 helices of neighboring subunits; the S4–S5 linker is decisive for gate opening. Gochman 2023: CBD sensitized rat TRPV2 to the synthetic agonist 2-APB by more than two orders of magnitude, but did not sensitize it to 40 °C. Qin 2008Cell / labAnimalPumroy 2019Molecular structure (lab)Gochman 2023Molecular structure (lab)Cell / lab
Expert level: method notes
Method note
Pumroy 2019: 6U88 (state 2, 3.2 Å) and 6U8A (state 1, 3.4 Å), bound ligand P0T = cannabidiol; ligand-free structures 6U84 and 6U86. Gochman 2023: 8SLX (1 CBD, 3.23 Å), 8SLY (2 CBD, 3.32 Å); a new small-molecule site in the pore, next to the reported CBD site; sensitization much weaker at TRPV1. All four CBD-bound structures are rat TRPV2; there is no CBD-bound structure of human TRPV2. None of the 12 PDB entries containing CBD (P0T) is 5-HT1A, TRPV1, GPR55 or PPARγ (October 24, 2026). Pumroy 2019Molecular structure (lab)Gochman 2023Molecular structure (lab)Cell / labPDB 6U88Molecular structure (lab)
Structure: CBD-bound rat TRPV2 in a nanodisc, cryo-EM 3.2 Å. Among these targets, the only structure in which CBD has been imaged in its bound state. Pumroy 2019Molecular structure (lab)PDB 6U88Molecular structure (lab) RCSB PDB 6U88
How lab concentrations compare with the level measured in blood, and CBD's other targets: CBD's other targets.
Identifiers and citation
- Protein
- Transient receptor potential cation channel subfamily V member 2 (gene TRPV2, human; UniProt Q9Y5S1)
- Structure
- RCSB PDB 6U88: CBD-bound rat TRPV2 in a nanodisc, cryo-EM 3.2 Å. Among these targets, the only structure in which CBD has been imaged in its bound state.
How to cite: cbd.school editorial team. CBD and TRPV2. Endocannabinoid system 3D map, cbd.school. Last updated October 24, 2026. https://cbd.school/learn/endocannabinoid-system-map/hedefler/trpv2/
Protein structure from RCSB PDB (CC0 1.0). The map, text and downloaded images are CC BY-SA 4.0. An independent expert review has not been done yet. All licenses
Other pages of the map
Overview: what the endocannabinoid system is, the feedback brake at the synapse, CBD's targets, lesson mode, data and licenses.
Sources
Show 5 references
- Caterina MJ, Rosen TA, Tominaga M, Brake AJ, Julius D. A capsaicin-receptor homologue with a high threshold for noxious heat. Nature. 1999;398(6726):436-41. PMID 10201375 · doi:10.1038/18906 Cell / labAnimal
- Qin N, Neeper MP, Liu Y et al. TRPV2 is activated by cannabidiol and mediates CGRP release in cultured rat dorsal root ganglion neurons. J Neurosci. 2008;28(24):6231-8. PMID 18550765 · doi:10.1523/JNEUROSCI.0504-08.2008 Cell / labAnimal
- Pumroy RA, Samanta A, Liu Y et al. Molecular mechanism of TRPV2 channel modulation by cannabidiol. Elife. 2019;8:e48792. PMID 31566564 · doi:10.7554/eLife.48792 Molecular structure (lab)
- Gochman A, Tan XF, Bae C et al. Cannabidiol sensitizes TRPV2 channels to activation by 2-APB. Elife. 2023;12:e86166. PMID 37199723 · doi:10.7554/eLife.86166 Molecular structure (lab)Cell / lab
- RCSB Protein Data Bank, entry 6U88: CBD-bound full-length rat TRPV2 in nanodiscs, state 2 (cryo-EM, 3.2 Å; bound P0T = cannabidiol). doi:10.2210/pdb6U88/pdb. PDB data CC0 1.0. · doi:10.2210/pdb6U88/pdb Molecular structure (lab)