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Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II
Open accessAbstract
G protein-coupled receptors (GPCR) are seven transmembrane helix proteins that couple binding of extracellular ligands to conformational changes and activation of intracellular G proteins, GPCR kinases, and arrestins. Constitutively active mutants are ubiquitously found among GPCRs and increase the inherent basal activity of the receptor, which often correlates with a pathological outcome. Here, we have used the M257Y 6.40 constitutively active mutant of the photoreceptor rhodopsin in combination with the specific binding of a C-terminal fragment from the G protein alpha subunit (GαCT) to trap a light activated state for crystallization. The structure of the M257Y/GαCT complex contains the agonist all- trans -retinal covalently bound to the native binding pocket and resembles the G protein binding metarhodopsin-II conformation obtained by the natural activation mechanism; i.e., illumination of the prebound chromophore 11- cis -retinal. The structure further suggests a molecular basis for the constitutive activity of 6.40 substitutions and the strong effect of the introduced tyrosine based on specific interactions with Y223 5.58 in helix 5, Y306 7.53 of the NPxxY motif and R135 3.50 of the E(D)RY motif, highly conserved residues of the G protein binding site.
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Cites
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
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
Crystal structure of opsin in its G-protein-interacting conformation
Scheerer, P., Park, J. H., Hildebrand, P. W., Kim, Y. J., Krauß, N., Choe, H.-W., Hofmann, K. P., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07330 · Cited by 1,059
Crystal structure of metarhodopsin II
Choe, H.-W., Kim, Y. J., Park, J. H., Morizumi, T., Pai, E. F., Krauß, N., Hofmann, K. P., Scheerer, P., & Ernst, O. P. (2011) · Nature · doi:10.1038/nature09789 · Cited by 663
Cited by
Molecular signatures of G-protein-coupled receptors
Venkatakrishnan, A. J., Deupi, X., Lebon, G., Tate, C. G., Schertler, G. F., & Babu, M. M. (2013) · Nature · doi:10.1038/nature11896 · Cited by 1,497
Self-citationMicrobial and Animal Rhodopsins: Structures, Functions, and Molecular Mechanisms
Ernst, O. P., Lodowski, D. T., Elstner, M., Hegemann, P., Brown, L. S., & Kandori, H. (2014) · Chemical Reviews · doi:10.1021/cr4003769 · Cited by 1,153
Activation and allosteric modulation of a muscarinic acetylcholine receptor
Kruse, A. C., Ring, A. M., Manglik, A., Hu, J., Hu, K., Eitel, K., Hübner, H., Pardon, E., Valant, C., Sexton, P. M., et al. (2013) · Nature · doi:10.1038/nature12735 · Cited by 893
Brunk, E., & Rothlisberger, U. (2015) · Chemical Reviews · doi:10.1021/cr500628b · Cited by 494
Universal allosteric mechanism for Gα activation by GPCRs
Flock, T., Ravarani, C. N. J., Sun, D., Venkatakrishnan, A. J., Kayikci, M., Tate, C. G., Veprintsev, D. B., & Babu, M. M. (2015) · Nature · doi:10.1038/nature14663 · Cited by 365
Metadata
- Authors
- Deupi, X., Edwards, P., Singhal, A., Nickle, B., Oprian, D., Schertler, G., & Standfuss, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2011-12-23
- Volume
- 109
- Issue
- 1
- Pages
- 119-124
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1999842541
- Cited by
- 242
- References
- 4
- FWCI
- 8.46
- Type
- journal article
- Language
- en
- Open access
- green
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- Deupi, X., Edwards, P., Singhal, A., Nickle, B., Oprian, D., Schertler, G., & Standfuss, J. (2012). Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1114089108
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