The DOI matches its Crossref record; 88 of the 88 references it cites were found in a registry or an index.
Allosteric sodium in class A GPCR signaling
Open accessAbstract
Despite their functional and structural diversity, G protein-coupled receptors (GPCRs) share a common mechanism of signal transduction via conformational changes in the seven-transmembrane (7TM) helical domain. New major insights into this mechanism come from the recent crystallographic discoveries of a partially hydrated sodium ion that is specifically bound in the middle of the 7TM bundle of multiple class A GPCRs. This review discusses the remarkable structural conservation and distinct features of the Na+ pocket in this most populous GPCR class, as well as the conformational collapse of the pocket on receptor activation. New insights help to explain allosteric effects of sodium on GPCR agonist binding and activation, and sodium’s role as a potential co-factor in class A GPCR function.
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Cites
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Self-citationCrystal structure of the β2 adrenergic receptor–Gs protein complex
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Self-citationTransduction of Receptor Signals by ß-Arrestins
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Cited by
Roth, B. L. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.040 · Cited by 1,742
Self-citationVerkhratsky, A., & Nedergaard, M. (2018) · Physiological Reviews · doi:10.1152/physrev.00042.2016 · Cited by 1,678
GPCR Dynamics: Structures in Motion
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Common activation mechanism of class A GPCRs
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
Self-citationPharmacogenomics of GPCR Drug Targets
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Metadata
- Authors
- Katritch, V., Fenalti, G., Abola, E. E., Roth, B. L., Cherezov, V., & Stevens, R. C.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2014-05
- Volume
- 39
- Issue
- 5
- Pages
- 233-244
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2067973462
- Cited by
- 511
- References
- 88
- FWCI
- 2.98
- Type
- journal article
- Language
- en
- Open access
- green
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