The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
High-resolution crystal structure of the human CB1 cannabinoid receptor
Open accessAbstract
The human cannabinoid G-protein-coupled receptors (GPCRs) CB1 and CB2 mediate the functional responses to the endocannabinoids anandamide and 2-arachidonyl glycerol (2-AG) and to the widely consumed plant phytocannabinoid Δ9-tetrahydrocannabinol (THC). The cannabinoid receptors have been the targets of intensive drug discovery efforts, because modulation of these receptors has therapeutic potential to control pain, epilepsy, obesity, and other disorders. Although much progress in understanding the biophysical properties of GPCRs has recently been made, investigations of the molecular mechanisms of the cannabinoids and their receptors have lacked high-resolution structural data. Here we report the use of GPCR engineering and lipidic cubic phase crystallization to determine the structure of the human CB1 receptor bound to the inhibitor taranabant at 2.6-Å resolution. We found that the extracellular surface of CB1, including the highly conserved membrane-proximal N-terminal region, is distinct from those of other lipid-activated GPCRs, forming a critical part of the ligand-binding pocket. Docking studies further demonstrate how this same pocket may accommodate the cannabinoid agonist THC. Our CB1 structure provides an atomic framework for studying cannabinoid receptor function and will aid the design and optimization of therapeutic modulators of the endocannabinoid system.
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[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Friesner, R. A., Banks, J. L., Murphy, R. B., Halgren, T. A., Klicic, J. J., Mainz, D. T., Repasky, M. P., Knoll, E. H., Shelley, M., Perry, J. K., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0306430 · Cited by 10,057
The Amber biomolecular simulation programs
Case, D. A., Cheatham, T. E., Darden, T., Gohlke, H., Luo, R., Merz, K. M., Onufriev, A., Simmerling, C., Wang, B., & Woods, R. J. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20290 · Cited by 9,535
Electrostatics of nanosystems: Application to microtubules and the ribosome
Baker, N. A., Sept, D., Joseph, S., Holst, M. J., & McCammon, J. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181342398 · Cited by 7,172
Friesner, R. A., Murphy, R. B., Repasky, M. P., Frye, L. L., Greenwood, J. R., Halgren, T. A., Sanschagrin, P. C., & Mainz, D. T. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm051256o · Cited by 6,851
Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637
PRODRG: a tool for high-throughput crystallography of protein–ligand complexes
Schüttelkopf, A. W., & van Aalten, D. M. F. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904011679 · Cited by 4,804
Isolation, Structure, and Partial Synthesis of an Active Constituent of Hashish
Gaoni, Y., & Mechoulam, R. (1964) · Journal of the American Chemical Society · doi:10.1021/ja01062a046 · Cited by 2,393
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Crystal Structure of the Human Cannabinoid Receptor CB1
Hua, T., Vemuri, K., Pu, M., Qu, L., Han, G. W., Wu, Y., Zhao, S., Shui, W., Li, S., Korde, A., et al. (2016) · Cell · doi:10.1016/j.cell.2016.10.004 · Cited by 673
Structure of a Signaling Cannabinoid Receptor 1-G Protein Complex
Krishna Kumar, K., Shalev-Benami, M., Robertson, M. J., Hu, H., Banister, S. D., Hollingsworth, S. A., Latorraca, N. R., Kato, H. E., Hilger, D., Maeda, S., et al. (2019) · Cell · doi:10.1016/j.cell.2018.11.040 · Cited by 419
Goods and Bads of the Endocannabinoid System as a Therapeutic Target: Lessons Learned after 30 Years
Maccarrone, M., Di Marzo, V., Gertsch, J., Grether, U., Howlett, A. C., Hua, T., Makriyannis, A., Piomelli, D., Ueda, N., & van der Stelt, M. (2023) · Pharmacological Reviews · doi:10.1124/pharmrev.122.000600 · Cited by 183
Cannabis sativa: Much more beyond Δ9-tetrahydrocannabinol
Alves, P., Amaral, C., Teixeira, N., & Correia-da-Silva, G. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104822 · Cited by 135
Spanagel, R. (2020) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2020.22.3/rspanagel · Cited by 127
Metadata
- Authors
- Shao, Z., Yin, J., Chapman, K., Grzemska, M., Clark, L., Wang, J., & Rosenbaum, D. M.
- Venue
- Nature
- Published
- 2016-11-16
- Volume
- 540
- Issue
- 7634
- Pages
- 602-606
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2553376712
- Cited by
- 419
- References
- 47
- FWCI
- 24.53
- Type
- journal article
- Language
- en
- Open access
- green
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- Shao, Z., Yin, J., Chapman, K., Grzemska, M., Clark, L., Wang, J., & Rosenbaum, D. M. (2016). High-resolution crystal structure of the human CB1 cannabinoid receptor. Nature. https://doi.org/10.1038/nature20613
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