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Structure of TRPV1 channel revealed by electron cryomicroscopy
Open accessAbstract
The transient receptor potential (TRP) family of ion channels participate in many signaling pathways. TRPV1 functions as a molecular integrator of noxious stimuli, including heat, low pH, and chemical ligands. Here, we report the 3D structure of full-length rat TRPV1 channel expressed in the yeast Saccharomyces cerevisiae and purified by immunoaffinity chromatography. We demonstrate that the recombinant purified TRPV1 channel retains its structural and functional integrity and is suitable for structural analysis. The 19-Å structure of TRPV1 determined by using single-particle electron cryomicroscopy exhibits fourfold symmetry and comprises two distinct regions: a large open basket-like domain, likely corresponding to the cytoplasmic N- and C-terminal portions, and a more compact domain, corresponding to the transmembrane portion. The assignment of transmembrane and cytoplasmic regions was supported by fitting crystal structures of the structurally homologous Kv1.2 channel and isolated TRPV1 ankyrin repeats into the TRPV1 structure.
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Cites
TRP channels as cellular sensors
Clapham, D. E. (2003) · Nature · doi:10.1038/nature02196 · Cited by 2,779
Cited by
Zhang, M., Ma, Y., Ye, X., Zhang, N., Pan, L., & Wang, B. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01464-x · Cited by 522
TRPV4: molecular conductor of a diverse orchestra
White, J. P. M., Cibelli, M., Urban, L., Nilius, B., McGeown, J. G., & Nagy, I. (2016) · Physiological Reviews · doi:10.1152/physrev.00016.2015 · Cited by 405
Transient Receptor Potential Channels in the Vasculature
Earley, S., & Brayden, J. E. (2015) · Physiological Reviews · doi:10.1152/physrev.00026.2014 · Cited by 420
Wu, X., Jiang, Y., Rommelfanger, N. J., Yang, F., Zhou, Q., Yin, R., Liu, J., Cai, S., Ren, W., Shin, A., et al. (2022) · Nature Biomedical Engineering · doi:10.1038/s41551-022-00862-w · Cited by 222
TRPV1 and Endocannabinoids: Emerging Molecular Signals that Modulate Mammalian Vision
Ryskamp, D., Redmon, S., Jo, A., & Križaj, D. (2014) · Cells · doi:10.3390/cells3030914 · Cited by 60
Metadata
- Authors
- Moiseenkova-Bell, V. Y., Stanciu, L. A., Serysheva, I. I., Tobe, B. J., & Wensel, T. G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-05-27
- Volume
- 105
- Issue
- 21
- Pages
- 7451-7455
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2077225258
- Cited by
- 216
- References
- 1
- FWCI
- 8.67
- Type
- journal article
- Language
- en
- Open access
- green
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- Moiseenkova-Bell, V. Y., Stanciu, L. A., Serysheva, I. I., Tobe, B. J., & Wensel, T. G. (2008). Structure of TRPV1 channel revealed by electron cryomicroscopy. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0711835105
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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