The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor
Open accessAbstract
Summary The kappa-opioid receptor (KOP) mediates the actions of opioids with hallucinogenic, dysphoric and analgesic activities. The design of KOP analgesics devoid of hallucinatory and dysphoric effects has been hindered by an incomplete structural and mechanistic understanding of KOP agonist actions. Here we provide a crystal structure of the human KOP in complex with the potent epoxymorphinan opioid agonist MP1104 and an active state stabilizing nanobody. Comparisons between inactive and active state opioid receptor structures reveal substantial conformational changes in the binding pocket, intracellular and extracellular regions. Extensive structural analysis and experimental validation illuminate key residues that propagate larger scale structural rearrangements and transducer binding that, collectively, elucidate the structural determinants of KOP pharmacology, function, and biased signaling. These molecular insights promise to accelerate the structure-guided design of safer and more effective kappa-opioid receptor therapeutics.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
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
GROMACS: Fast, flexible, and free
Van Der Spoel, D., Lindahl, E., Hess, B., Groenhof, G., Mark, A. E., & Berendsen, H. J. C. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20291 · Cited by 19,182
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,742
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334
Best, R. B., Zhu, X., Shim, J., Lopes, P. E. M., Mittal, J., Feig, M., & MacKerell, A. D. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300400x · Cited by 4,532
Lee, J., Cheng, X., Swails, J. M., Yeom, M. S., Eastman, P. K., Lemkul, J. A., Wei, S., Buckner, J., Jeong, J. C., Qi, Y., et al. (2016) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00935 · Cited by 4,171
Crystal structure of the β2 adrenergic receptor–Gs protein complex
Rasmussen, S. G. F., DeVree, B. T., Zou, Y., Kruse, A. C., Chung, K. Y., Kobilka, T. S., Thian, F. S., Chae, P. S., Pardon, E., Calinski, D., et al. (2011) · Nature · doi:10.1038/nature10361 · Cited by 3,009
Self-citation
Cited by
Structure of a Hallucinogen-Activated Gq-Coupled 5-HT2A Serotonin Receptor
Kim, K., Che, T., Panova, O., DiBerto, J. F., Lyu, J., Krumm, B. E., Wacker, D., Robertson, M. J., Seven, A. B., Nichols, D. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.024 · Cited by 481
Self-citationUntangling the complexity of opioid receptor function
Valentino, R. J., & Volkow, N. D. (2018) · Neuropsychopharmacology · doi:10.1038/s41386-018-0225-3 · Cited by 383
PtdIns(4,5)P2 stabilizes active states of GPCRs and enhances selectivity of G-protein coupling
Yen, H.-Y., Hoi, K. K., Liko, I., Hedger, G., Horrell, M. R., Song, W., Wu, D., Heine, P., Warne, T., Lee, Y., et al. (2018) · Nature · doi:10.1038/s41586-018-0325-6 · Cited by 284
Massaly, N., Copits, B. A., Wilson-Poe, A. R., Hipólito, L., Markovic, T., Yoon, H. J., Liu, S., Walicki, M. C., Bhatti, D. L., Sirohi, S., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.02.029 · Cited by 200
Bloch, J. S., Mukherjee, S., Kowal, J., Filippova, E. V., Niederer, M., Pardon, E., Steyaert, J., Kossiakoff, A. A., & Locher, K. P. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2115435118 · Cited by 114
Self-citation
Metadata
- Authors
- Che, T., Majumdar, S., Zaidi, S. A., Ondachi, P., McCorvy, J. D., Wang, S., Mosier, P. D., Uprety, R., Vardy, E., Krumm, B. E., Han, G. W., Lee, M.-Y., Pardon, E., Steyaert, J., Huang, X.-P., Strachan, R. T., Tribo, A. R., Pasternak, G. W., Carroll, F. I., Stevens, R. C., Cherezov, V., Katritch, V., Wacker, D., & Roth, B. L.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2018-01
- Volume
- 172
- Issue
- 1-2
- Pages
- 55-67.e15
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2781483269
- Cited by
- 365
- References
- 73
- FWCI
- 17.26
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor. https://app.cochat.ai/papers/10.1016/j.cell.2017.12.011
- The paper
- Che, T., Majumdar, S., Zaidi, S. A., Ondachi, P., McCorvy, J. D., Wang, S., Mosier, P. D., Uprety, R., Vardy, E., Krumm, B. E., Han, G. W., Lee, M.-Y., Pardon, E., Steyaert, J., Huang, X.-P., Strachan, R. T., Tribo, A. R., Pasternak, G. W., Carroll, F. I., . . . Roth, B. L. (2018). Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor. Cell. https://doi.org/10.1016/j.cell.2017.12.011
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
