The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Mini-G proteins: Novel tools for studying GPCRs in their active conformation
Open accessAbstract
Mini-G proteins are the engineered GTPase domains of Gα subunits. They couple to GPCRs and recapitulate the increase in agonist affinity observed upon coupling of a native heterotrimeric G protein. Given the small size and stability of mini-G proteins, and their ease of expression and purification, they are ideal for biophysical studies of GPCRs in their fully active state. The first mini-G protein developed was mini-Gs. Here we extend the family of mini-G proteins to include mini-Golf, mini-Gi1, mini-Go1 and the chimeras mini-Gs/q and mini-Gs/i. The mini-G proteins were shown to couple to relevant GPCRs and to form stable complexes with purified receptors that could be purified by size exclusion chromatography. Agonist-bound GPCRs coupled to a mini-G protein showed higher thermal stability compared to the agonist-bound receptor alone. Fusion of GFP at the N-terminus of mini-G proteins allowed receptor coupling to be monitored by fluorescence-detection size exclusion chromatography (FSEC) and, in a separate assay, the affinity of mini-G protein binding to detergent-solubilised receptors was determined. This work provides the foundation for the development of any mini-G protein and, ultimately, for the structure determination of GPCRs in a fully active state.
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Cites
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
The structure and function of G-protein-coupled receptors
Rosenbaum, D. M., Rasmussen, S. G. F., & Kobilka, B. K. (2009) · Nature · doi:10.1038/nature08144 · Cited by 2,534
Structure of a nanobody-stabilized active state of the β2 adrenoceptor
Rasmussen, S. G. F., Choi, H.-J., Fung, J. J., Pardon, E., Casarosa, P., Chae, P. S., DeVree, B. T., Rosenbaum, D. M., Thian, F. S., Kobilka, T. S., et al. (2011) · Nature · doi:10.1038/nature09648 · Cited by 1,680
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-citationStructure of a β1-adrenergic G-protein-coupled receptor
Warne, T., Serrano-Vega, M. J., Baker, J. G., Moukhametzianov, R., Edwards, P. C., Henderson, R., Leslie, A. G. W., Tate, C. G., & Schertler, G. F. X. (2008) · Nature · doi:10.1038/nature07101 · Cited by 1,344
Self-citationCrystal 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 the ligand-free G-protein-coupled receptor opsin
Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H.-W., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07063 · Cited by 903
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
Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation
Lebon, G., Warne, T., Edwards, P. C., Bennett, K., Langmead, C. J., Leslie, A. G. W., & Tate, C. G. (2011) · Nature · doi:10.1038/nature10136 · Cited by 873
Self-citationStructure of an Agonist-Bound Human A 2A Adenosine Receptor
Xu, F., Wu, H., Katritch, V., Han, G. W., Jacobson, K. A., Gao, Z.-G., Cherezov, V., & Stevens, R. C. (2011) · Science · doi:10.1126/science.1202793 · Cited by 813
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Zhou, Q., Yang, D., Wu, M., Guo, Y., Guo, W., Zhong, L., Cai, X., Dai, A., Jang, W., Shakhnovich, E. I., et al. (2019) · eLife · doi:10.7554/elife.50279 · Cited by 632
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
Impact of GPCR Structures on Drug Discovery
Congreve, M., de Graaf, C., Swain, N. A., & Tate, C. G. (2020) · Cell · doi:10.1016/j.cell.2020.03.003 · Cited by 375
Self-citationPtdIns(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
Self-citationNative Mass Spectrometry of Membrane Proteins
Keener, J. E., Zhang, G., & Marty, M. T. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c04342 · Cited by 126
Metadata
- Authors
- Nehmé, R., Carpenter, B., Singhal, A., Strege, A., Edwards, P. C., White, C. F., Du, H., Grisshammer, R., & Tate, C. G.
- Venue
- PLOS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2017-04-20
- Volume
- 12
- Issue
- 4
- Pages
- e0175642
- ISSN
- 1932-6203 (ISSN-L)
- OpenAlex
- W2605671347
- Cited by
- 323
- References
- 48
- FWCI
- 4.95
- Type
- journal article
- Language
- en
- Open access
- gold
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- Nehmé, R., Carpenter, B., Singhal, A., Strege, A., Edwards, P. C., White, C. F., Du, H., Grisshammer, R., & Tate, C. G. (2017). Mini-G proteins: Novel tools for studying GPCRs in their active conformation. PLOS ONE. https://doi.org/10.1371/journal.pone.0175642
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