The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Effects of Mg2+ and the beta gamma-subunit complex on the interactions of guanine nucleotides with G proteins.
Open accessAbstract
Mg2+ interacts with the alpha subunits of guanine nucleotide-binding regulatory proteins (G proteins) in the presence of guanosine-5'-[gamma-thio]triphosphate (GTP-gamma S) to form a highly fluorescent complex from which nucleotide dissociates very slowly. The apparent Kd for interaction of G alpha X GTP gamma S with Mg2+ is approximately 5 nM, similar to the Km for G protein GTPase activity X G beta gamma increases the rate of dissociation of GTP gamma S from G alpha X GTP gamma S or G alpha X GTP gamma S X Mg2+ at low concentrations of Mg2+. When the concentration of Mg2+ exceeds 1 mM, G beta gamma dissociates from G beta gamma X G alpha X GTP gamma S X Mg2+. Compared with the dramatic effect of Mg2+ on binding of GTP gamma S to G alpha, the metal has relatively little effect on the binding of GDP. However, G beta gamma increases the affinity of G alpha for GDP by more than 100-fold. High concentrations of Mg2+ promote the dissociation of GDP from G beta gamma X G alpha X GDP, apparently without causing subunit dissociation. The steady-state rate of GTP hydrolysis is strictly correlated with the rate of dissociation of GDP from G alpha under all conditions examined. Thus, there are at least two sites for interaction of Mg2+ with G protein-nucleotide complexes. Furthermore, binding of G beta gamma and GTP gamma S to G alpha is negatively cooperative, while the binding interaction between G beta gamma and GDP is strongly positive.
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Cites
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Self-citationThe regulatory component of adenylate cyclase. Purification and properties.
Sternweis, P. C., Northup, J. K., Smigel, M. D., & Gilman, A. G. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68431-0 · Cited by 508
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Self-citationThe influence of bound GDP on the kinetics of guanine nucleotide binding to G proteins.
Ferguson, K. M., Higashijima, T., Smigel, M. D., & Gilman, A. G. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38404-1 · Cited by 259
Self-citationThe effect of GTP and Mg2+ on the GTPase activity and the fluorescent properties of Go.
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Cited by
The GTPase superfamily: conserved structure and molecular mechanism
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Receptor-effector coupling by G proteins
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Structure and dynamics of GPCR signaling complexes
Hilger, D., Masureel, M., & Kobilka, B. K. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0011-7 · Cited by 969
Gz, a guanine nucleotide-binding protein with unique biochemical properties.
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Metadata
- Authors
- Higashijima, T., Ferguson, K. M., Sternweis, P. C., Smigel, M. D., & Gilman, A. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1987-01
- Volume
- 262
- Issue
- 2
- Pages
- 762-766
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1499695147
- Cited by
- 366
- References
- 11
- FWCI
- 7.40
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Higashijima, T., Ferguson, K. M., Sternweis, P. C., Smigel, M. D., & Gilman, A. G. (1987). Effects of Mg2+ and the beta gamma-subunit complex on the interactions of guanine nucleotides with G proteins. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)75851-7
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