The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Universal allosteric mechanism for Gα activation by GPCRs
Open accessAbstract
G protein-coupled receptors (GPCRs) allosterically activate heterotrimeric G proteins and trigger GDP release. Given that there are ∼800 human GPCRs and 16 different Gα genes, this raises the question of whether a universal allosteric mechanism governs Gα activation. Here we show that different GPCRs interact with and activate Gα proteins through a highly conserved mechanism. Comparison of Gα with the small G protein Ras reveals how the evolution of short segments that undergo disorder-to-order transitions can decouple regions important for allosteric activation from receptor binding specificity. This might explain how the GPCR–Gα system diversified rapidly, while conserving the allosteric activation mechanism.
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Metadata
- Authors
- Flock, T., Ravarani, C. N. J., Sun, D., Venkatakrishnan, A. J., Kayikci, M., Tate, C. G., Veprintsev, D. B., & Babu, M. M.
- Venue
- Nature
- Published
- 2015-07-06
- Volume
- 524
- Issue
- 7564
- Pages
- 173-179
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1199870172
- Cited by
- 365
- References
- 68
- FWCI
- 11.96
- Type
- journal article
- Language
- en
- Open access
- green
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- Flock, T., Ravarani, C. N. J., Sun, D., Venkatakrishnan, A. J., Kayikci, M., Tate, C. G., Veprintsev, D. B., & Babu, M. M. (2015). Universal allosteric mechanism for Gα activation by GPCRs. Nature. https://doi.org/10.1038/nature14663
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