Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Article
  • Published:

Structures of TRPV2 in distinct conformations provide insight into role of the pore turret

Nature Structural & Molecular Biology volume 26, pages 40–49 (2019)Cite this article

Subjects

Abstract

Cation channels of the transient receptor potential (TRP) family serve important physiological roles by opening in response to diverse intra- and extracellular stimuli that regulate their lower or upper gates. Despite extensive studies, the mechanism coupling these gates has remained obscure. Previous structures have failed to resolve extracellular loops, known in the TRPV subfamily as ‘pore turrets’, which are proximal to the upper gates. We established the importance of the pore turret through activity assays and by solving structures of rat TRPV2, both with and without an intact turret at resolutions of 4.0 Å and 3.6 Å, respectively. These structures resolve the full-length pore turret and reveal fully open and partially open states of TRPV2, both with unoccupied vanilloid pockets. Our results suggest a mechanism by which physiological signals, such as lipid binding, can regulate the lower gate and couple to the upper gate through a pore-turret-facilitated mechanism.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Fig. 1: Effects of pore turret deletions and phosphoinositides on channel activity.
Fig. 2: TRPV2 constructs and cryo-EM density maps.
Fig. 3: Structure and orientation of pore turret domain.
Fig. 4: Cation pathway of WT and mutant variants of TRPV2.
Fig. 5: Comparisons of TRPV2 structures.
Fig. 6: Model alignments of S3–S6.
Fig. 7: Model mechanism for agonist-independent TRPV2 activation.

Similar content being viewed by others

Data availability

The rat TRPV2 models (PDB 6BO4 (WT) and PDB 6BO5 (mutant)) and cryo-EM density maps (EMD-7118 (WT) and EMD-7119 (mutant)) have been deposited in the PDB (http://www.rcsb.org/) and the Electron Microscopy Data Bank (https://www.ebi.ac.uk/pdbe/emdb/). Other data are available from the corresponding authors upon reasonable request.

References

  1. Clapham, D. E. TRP channels as cellular sensors. Nature 426, 517–524 (2003).

    Article  CAS  PubMed  Google Scholar 

  2. Clapham, D. E., Runnels, L. W. & Strubing, C. The TRP ion channel family. Nat. Rev. Neurosci. 2, 387–396 (2001).

    Article  CAS  PubMed  Google Scholar 

  3. Montell, C. et al. A unified nomenclature for the superfamily of TRP cation channels. Mol. Cell 9, 229–231 (2002).

    Article  CAS  PubMed  Google Scholar 

  4. Jordt, S. E. & Ehrlich, B. E. TRP channels in disease. Subcell. Biochem. 45, 253–271 (2007).

    Article  CAS  PubMed  Google Scholar 

  5. Nilius, B. TRP channels in disease. Biochim. Biophys. Acta 1772, 805–812 (2007).

    Article  CAS  PubMed  Google Scholar 

  6. Nilius, B. et al. Gating of TRP channels: a voltage connection? J. Physiol. 567, 35–44 (2005).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  7. Li, M., Yu, Y. & Yang, J. Structural biology of TRP channels. Adv. Exp. Med. Biol. 704, 1–23 (2011).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  8. Kaneko, Y. & Szallasi, A. Transient receptor potential (TRP) channels: a clinical perspective. Br. J. Pharmacol. 171, 2474–2507 (2014).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  9. Wong, G. Y. & Gavva, N. R. Therapeutic potential of vanilloid receptor TRPV1 agonists and antagonists as analgesics: recent advances and setbacks. Brain Res. Rev. 60, 267–277 (2009).

    Article  CAS  PubMed  Google Scholar 

  10. Carnevale, V. & Rohacs, T. TRPV1: A target for rational drug design. Pharmaceuticals (Basel) 9, 52 (2016).

    Article  Google Scholar 

  11. Reilly, R. M. et al. Pharmacology of modality-specific transient receptor potential vanilloid-1 antagonists that do not alter body temperature. J. Pharmacol. Exp. Ther. 342, 416–428 (2012).

    Article  CAS  PubMed  Google Scholar 

  12. Brown, W. et al. Safety, pharmacokinetics, and pharmacodynamics study in healthy subjects of oral NEO6860, a modality selective transient receptor potential vanilloid subtype 1 antagonist. J. Pain 18, 726–738 (2017).

    Article  CAS  PubMed  Google Scholar 

  13. Gao, Y., Cao, E., Julius, D. & Cheng, Y. TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action. Nature 534, 347–351 (2016).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  14. Cao, E., Liao, M., Cheng, Y. & Julius, D. TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504, 113–118 (2013).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  15. Liao, M., Cao, E., Julius, D. & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107–112 (2013).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  16. Huynh, K. W. et al. Structure of the full-length TRPV2 channel by cryo-EM. Nat. Commun. 7, 11130 (2016).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  17. Zubcevic, L. et al. Cryo-electron microscopy structure of the TRPV2 ion channel. Nat. Struct. Mol. Biol. 23, 180–186 (2016).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  18. Saotome, K., Singh, A. K., Yelshanskaya, M. V. & Sobolevsky, A. I. Crystal structure of the epithelial calcium channel TRPV6. Nature 534, 506–511 (2016).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  19. Yin, Y. et al. Structure of the cold- and menthol-sensing ion channel TRPM8. Science 359, 237–241 (2018).

    Article  CAS  PubMed  Google Scholar 

  20. Zubcevic, L., Le, S., Yang, H. & Lee, S. Y. Conformational plasticity in the selectivity filter of the TRPV2 ion channel. Nat. Struct. Mol. Biol. 25, 405–415 (2018).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  21. Yang, F., Cui, Y., Wang, K. & Zheng, J. Thermosensitive TRP channel pore turret is part of the temperature activation pathway. Proc. Natl Acad. Sci. USA 107, 7083–7088 (2010).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  22. Cui, Y. et al. Selective disruption of high sensitivity heat activation but not capsaicin activation of TRPV1 channels by pore turret mutations. J. Gen. Physiol. 139, 273–283 (2012).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  23. Yang, F., Ma, L., Cao, X., Wang, K. & Zheng, J. Divalent cations activate TRPV1 through promoting conformational change of the extracellular region. J. Gen. Physiol. 143, 91–103 (2014).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  24. Winter, Z. et al. Functionally important amino acid residues in the transient receptor potential vanilloid 1 (TRPV1) ion channel−an overview of the current mutational data. Mol. Pain 9, 30 (2013).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  25. Jara-Oseguera, A., Bae, C. & Swartz, K. J. An external sodium ion binding site controls allosteric gating in TRPV1 channels. Elife 5, e13356 (2016).

    Article  PubMed  PubMed Central  Google Scholar 

  26. Jordt, S. E., Tominaga, M. & Julius, D. Acid potentiation of the capsaicin receptor determined by a key extracellular site. Proc. Natl Acad. Sci. USA 97, 8134–8139 (2000).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  27. Ryu, S., Liu, B., Yao, J., Fu, Q. & Qin, F. Uncoupling proton activation of vanilloid receptor TRPV1. J. Neurosci. 27, 12797–12807 (2007).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  28. Munns, C. H., Chung, M. K., Sanchez, Y. E., Amzel, L. M. & Caterina, M. J. Role of the outer pore domain in transient receptor potential vanilloid 1 dynamic permeability to large cations. J. Biol. Chem. 290, 5707–5724 (2015).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  29. Yang, F., Vu, S., Yarov-Yarovoy, V. & Zheng, J. Rational design and validation of a vanilloid-sensitive TRPV2 ion channel. Proc. Natl Acad. Sci. USA 113, E3657–E3666 (2016).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  30. Zhang, F. et al. Engineering vanilloid-sensitivity into the rat TRPV2 channel. eLife 5, e16409 (2016).

    Article  PubMed  PubMed Central  Google Scholar 

  31. Cao, E., Cordero-Morales, J. F., Liu, B., Qin, F. & Julius, D. TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids. Neuron 77, 667–679 (2013).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  32. Doerner, J. F., Hatt, H. & Ramsey, I. S. Voltage- and temperature-dependent activation of TRPV3 channels is potentiated by receptor-mediated PI(4,5)P2 hydrolysis. J. Gen. Physiol. 137, 271–288 (2011).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  33. Mercado, J., Gordon-Shaag, A., Zagotta, W. N. & Gordon, S. E. Ca2+-dependent desensitization of TRPV2 channels is mediated by hydrolysis of phosphatidylinositol 4,5-bisphosphate. J. Neurosci. 30, 13338–13347 (2010).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  34. Lukacs, V. et al. Dual regulation of TRPV1 by phosphoinositides. J. Neurosci. 27, 7070–7080 (2007).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  35. Rohacs, T. Phosphoinositide regulation of TRPV1 revisited. Pflugers Arch. 467, 1851–1869 (2015).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  36. Ufret-Vincenty, C. A. et al. Mechanism for phosphoinositide selectivity and activation of TRPV1 ion channels. J. Gen. Physiol. 145, 431–442 (2015).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  37. Suh, B. C., Inoue, T., Meyer, T. & Hille, B. Rapid chemically induced changes of PtdIns(4,5)P2 gate KCNQ ion channels. Science 314, 1454–1457 (2006).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  38. Klein, R. M., Ufret-Vincenty, C. A., Hua, L. & Gordon, S. E. Determinants of molecular specificity in phosphoinositide regulation. Phosphatidylinositol (4,5)-bisphosphate (PI(4,5)P2) is the endogenous lipid regulating TRPV1. J. Biol. Chem. 283, 26208–26216 (2008).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  39. Ramachandran, G. N., Ramakrishnan, C. & Sasisekharan, V. Stereochemistry of polypeptide chain configurations. J. Mol. Biol. 7, 95–99 (1963).

    Article  CAS  PubMed  Google Scholar 

  40. Smart, O. S., Neduvelil, J. G., Wang, X., Wallace, B. A. & Sansom, M. S. HOLE: a program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graph. 14, 354–360 (1996).

    Article  CAS  PubMed  Google Scholar 

  41. Matta, J. A. & Ahern, G. P. Voltage is a partial activator of rat thermosensitive TRP channels. J. Physiol. 585, 469–482 (2007).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  42. Jin, X., Touhey, J. & Gaudet, R. Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel. J. Biol. Chem. 281, 25006–25010 (2006).

    Article  CAS  PubMed  Google Scholar 

  43. McCleverty, C. J., Koesema, E., Patapoutian, A., Lesley, S. A. & Kreusch, A. Crystal structure of the human TRPV2 channel ankyrin repeat domain. Protein Sci. 15, 2201–2206 (2006).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  44. Sotomayor, M., Corey, D. P. & Schulten, K. In search of the hair-cell gating spring elastic properties of ankyrin and cadherin repeats. Structure 13, 669–682 (2005).

    Article  CAS  PubMed  Google Scholar 

  45. Lee, G. et al. Nanospring behaviour of ankyrin repeats. Nature 440, 246–249 (2006).

    Article  CAS  PubMed  Google Scholar 

  46. Gaudet, R. A primer on ankyrin repeat function in TRP channels and beyond. Mol. Biosyst. 4, 372–379 (2008).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  47. Corey, D. P. & Sotomayor, M. Hearing: tightrope act. Nature 428, 901–903 (2004).

    Article  CAS  PubMed  Google Scholar 

  48. Gavva, N. R. et al. Molecular determinants of vanilloid sensitivity in TRPV1. J. Biol. Chem. 279, 20283–20295 (2004).

    Article  CAS  PubMed  Google Scholar 

  49. Voets, T. et al. The principle of temperature-dependent gating in cold- and heat-sensitive TRP channels. Nature 430, 748–754 (2004).

    Article  CAS  PubMed  Google Scholar 

  50. Loukin, S., Su, Z., Zhou, X. & Kung, C. Forward genetic analysis reveals multiple gating mechanisms of TRPV4. J. Biol. Chem. 285, 19884–19890 (2010).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  51. Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10, 584–590 (2013).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  52. Mindell, J. A. & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334–347 (2003).

    Article  PubMed  Google Scholar 

  53. Henderson, R. et al. Outcome of the first electron microscopy validation task force meeting. Structure 20, 205–214 (2012).

    Article  CAS  PubMed  Google Scholar 

  54. Scheres, S. H. & Chen, S. Prevention of overfitting in cryo-EM structure determination. Nat. Methods 9, 853–854 (2012).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  55. Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519–530 (2012).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  56. Pettersen, E. F. et al. UCSF Chimera–a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004).

    Article  CAS  PubMed  Google Scholar 

  57. Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nat. Methods 11, 63–65 (2014).

    Article  CAS  PubMed  Google Scholar 

  58. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D Biol. Crystallogr. 66, 486–501 (2010).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  59. Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, (213–221 (2010).

    Google Scholar 

  60. Hryc, C. F. et al. Accurate model annotation of a near-atomic resolution cryo-EM map. Proc. Natl Acad. Sci. USA 114, 3103–3108 (2017).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  61. Barad, B. A. et al. EMRinger: side chain-directed model and map validation for 3D cryo-electron microscopy. Nat. Methods 12, 943–946 (2015).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

Download references

Acknowledgements

We thank C. Hryc for providing his expertise in modeling cryo-EM density maps and helping to validate the models. We thank M. Agosto, J. Gonzalez, and other members of the Wensel laboratory for helpful discussions and suggestions and M. Zhou for helpful comments. We thank the National Center for Macromolecular Imaging for providing the cryo-EM and computational resources. This work was supported by the Robert Welch Foundation (grant nos. Q0035 and Q-1967-20180324) and a training fellowship from the Houston Area Molecular Biophysics Program of the Keck Center of the Gulf Coast Consortia, National Institute of General Medical Sciences (grant no. T32GM008280). Further support was provided by National Institutes of Health grants (nos. P41GM103832, R01GM072804, R01EY007981, R01EY026545) and the American Heart Association (grant no. 16GRNT29720001).

Author information

Author notes

  1. These authors contributed equally: Timothy L. Dosey, Zhao Wang.

Authors and Affiliations

  1. Verna and Marrs Mclean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA

    Timothy L. Dosey, Zhao Wang, Zhixian Zhang, Wah Chiu & Theodore G. Wensel

  2. Department of Biochemistry and Molecular Biology, Structural Biology Imaging Center, McGovern Medical School at the University of Texas Health Science Center at Houston, Houston, TX, USA

    Guizhen Fan & Irina I. Serysheva

  3. Departments of Bioengineering and of Microbiology and Immunology, Stanford University, Stanford, CA, USA

    Wah Chiu

Authors
  1. Timothy L. Dosey
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Zhao Wang
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Guizhen Fan
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Zhixian Zhang
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Irina I. Serysheva
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Wah Chiu
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Theodore G. Wensel
    View author publications

    You can also search for this author in PubMed Google Scholar

Contributions

T.L.D. designed the project, designed and performed all biochemistry and molecular biology experiments, processed cryo-EM data, constructed and optimized the molecular models, prepared figures and animations, and wrote the manuscript. Z.W. and G.F. collected cryo-E.M. data, and Z.W. reconstructed, refined, and validated the maps. Z.Z. collected and processed preliminary cryo-EM data to optimize cryo-specimen preparation for high-resolution imaging. T.G.W., W.C., and I.I.S. supervised personnel, provided laboratory resources and facilities, participated in structure interpretations, and edited the manuscript.

Corresponding authors

Correspondence to Wah Chiu or Theodore G. Wensel.

Ethics declarations

Competing interests

The authors declare no competing interests.

Additional information

Publisher’s note: Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Integrated supplementary information

Supplementary Figure 1 Comparisons of the TRPV2 pore conformations and S6 registers and rearrangements of the upper gates for TRPV2 and TRPV1.

a,b, Van der Waals space filling representation of the pores for the previously deposited TRPV2 structures PDB 5HI9 (dark gray) and PDB 5AN8 (light gray), both showing fully closed conformations. c, Selectivity filter and pore loop region of the WT (blue) and mutant (purple) models fit to cryo-EM densities (mesh) indicating side chain positions. Included is a zoomed view of the M607 side chain responsible for blocking conduction at the upper gate. d, Cell-based TRPV2 activity assay showing that alanine substitution at L610 and F618 results in greatly diminished channel activity in response to 2-APB. e, Superimposition of closed TRPV1 (orange) (PDB 5IRZ) and open TRPV1 (pink) (PDB 5IRX). f, Superimposition of the open upper gates for our WT TRPV2 (blue) cryo-EM structure and the TRPV2 crystal structure (yellow) (PDB 6BWM).

Supplementary Figure 2 Optimization of constructs for heterologous expression and purification.

a, Diagrams for the TRPV2 (blue) and TRPV4 (orange) constructs created for a S. cerevisiae heterologous expression system. b, Western blot against the 1D4 epitope tag testing the relative expression levels of the indicated TRPV2 and TRPV4 constructs. Each well was loaded with an equal amount of yeast cells. d, Coomassie-stained gels with bands indicating the approximate molecular weights for the purified TRPV2 variant monomers. e, Size exclusion chromatography profiles for the purified TRPV2 variants. Fractions under the main peak were pooled for biochemical analysis and structure determination. f, Dose responses for the final TRPV2 constructs used for structure determination compared to the responses of the minimally modified counterparts.

Supplementary Figure 3 Resolution estimation of cryo-EM structures.

a,d, Resolution maps for the full-length (a) and mutant (d) TRPV2 variants. b,e, The overall resolutions for the full-length and mutant TRPV2 maps are 4 Å and 3.6 Å, respectively, and these were determined using Fourier shell correlations with a 0.143 cutoff. c,f, Representative areas of the TRPV2 maps (mesh) superimposed with the molecular models showing resolved α-helices with clear side chains in the ankyrin-repeat domain (ARD) and in the transmembrane domains. g,h, FSC curves for WT (g) and mutant (h) models versus half maps and the whole maps.

Supplementary Figure 4 Resolution estimation of cryo-EM structures.

a,d, Resolution maps for the full-length (a) and mutant (d) TRPV2 variants. b,e, The overall resolutions for the full-length and mutant TRPV2 maps are 4 Å and 3.6 Å, respectively, and these were determined using Fourier shell correlations with a 0.143 cutoff. c,f, Representative areas of the TRPV2 maps (mesh) superimposed with the molecular models showing resolved α-helices with clear side chains in the ankyrin-repeat domain (ARD) and in the transmembrane domains. g,h, FSC curves for WT (g) and mutant (h) models versus half maps and the whole maps.

Supplementary Figure 5 Pore turret model fit to density.

Rotated views of the pore turret loop backbone (green) fit to the density (mesh). Residues P565, P568, P579, P587, and P589 are labeled.

Supplementary Figure 6 Calculated atomic displacement parameters (also known as B factors) for the TRPV2 models.

a,e, Side and top views for the WT (a) and mutant (e) TRPV2 models color-coded according to the average atomic displacement parameter at each residue. b,f, Zoomed view of the WT (b) and mutant (f) TRPV2 pore regions. c,g, Side views of the WT (c) and mutant (g) TRPV2 monomer models. d,h, Zoom view of the WT (d) and mutant (h) lower gate and vanilloid pocket regions.

Supplementary Figure 7 S6 helix registers and TRPV1/TRPV2 lower gate conformation comparisons.

a, WT (blue) and mutant (purple) TRPV2 models for the S6 helix fit to cryo-EM densities (mesh). b, Superimposition of the S6 helices of WT and mutant TRPV2. c, Superimposition of WT TRPV2 S6 helix in the open conformation with the S6 helix of TRPV2 (5AN8) (gray) in the closed conformation. d, Lower gate superimpositions of the closed TRPV1 (orange) (PDB 5IRZ) conformation with the open conformation of DkTx/RTX-bound TRPV1 (pink) (PDB 5IRX). e, Lower gate superimpositions of the closed TRPV2 (5AN8) (gray) conformation with the open conformation of RTX-bound TRPV2 (yellow) (PDB 6BWM).

Supplementary information

Supplementary Text and Figures

Supplementary Figures 1–7

Reporting Summary

Supplementary Video 1

TRPV2 WT and mutant constructs and structures

Supplementary Video 2

TRPV2 pore turret structure

Supplementary Video 3

Proposed TRPV2 gating mechanism

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Dosey, T.L., Wang, Z., Fan, G. et al. Structures of TRPV2 in distinct conformations provide insight into role of the pore turret. Nat Struct Mol Biol 26, 40–49 (2019). https://doi.org/10.1038/s41594-018-0168-8

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/s41594-018-0168-8

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing