The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
G PROTEIN MECHANISMS: Insights from Structural Analysis
Abstract
This review is concerned with the structures and mechanisms of a superfamily of regulatory GTP hydrolases (G proteins). G proteins include Ras and its close homologs, translation elongation factors, and heterotrimeric G proteins. These proteins share a common structural core, exemplified by that of p21 ras (Ras), and significant sequence identity, suggesting a common evolutionary origin. Three-dimensional structures of members of the G protein superfamily are considered in light of other biochemical findings about the function of these proteins. Relationships among G protein structures are discussed, and factors contributing to their low intrinsic rate of GTP hydrolysis are considered. Comparison of GTP- and GDP-bound conformations of G proteins reveals how specific contacts between the γ-phosphate of GTP and the switch II region stabilize potential effector-binding sites and how GTP hydrolysis results in collapse (or reordering) of these surfaces. A GTPase-activating protein probably binds to and stabilizes the conformation of its cognate G protein that recognizes the transition state for hydrolysis, and may insert a catalytic residue into the G protein active site. Inhibitors of nucleotide release, such as the β γ subunit of a heterotrimeric G protein, bind selectively to and stabilize the GDP-bound state. Release factors, such as the translation elongation factor, Ts, also recognize the switch regions and destabilize the Mg 2+-binding site, thereby promoting GDP release. G protein–coupled receptors are expected to operate by a somewhat different mechanism, given that the GDP-bound form of many G protein α subunits does not contain bound Mg 2+.
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Cites
The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392
A Cytoplasmic Protein Stimulates Normal N- ras p21 GTPase, But Does Not Affect Oncogenic Mutants
Trahey, M., & McCormick, F. (1987) · Science · doi:10.1126/science.2821624 · Cited by 1,211
Kinetics of interaction of nucleotides with nucleotide-free H-ras p21
John, J., Sohmen, R., Feuerstein, J., Linke, R., Wittinghofer, A., & Goody, R. S. (1990) · Biochemistry · doi:10.1021/bi00477a025 · Cited by 429
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Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
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Vetter, I. R., & Wittinghofer, A. (2001) · Science · doi:10.1126/science.1062023 · Cited by 1,875
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Kumar, S., Ma, B., Tsai, C., Sinha, N., & Nussinov, R. (2000) · Protein Science · doi:10.1110/ps.9.1.10 · Cited by 595
Regulation, signaling, and physiological functions of G-Proteins
Syrovatkina, V., Alegre, K. O., Dey, R., & Huang, X.-Y. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.002 · Cited by 498
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Lau, C. K. Y., Krewulak, K. D., & Vogel, H. J. (2016) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv049 · Cited by 428
Caplan, S., Naslavsky, N., Hartnell, L. M., Lodge, R., Polishchuk, R. S., Donaldson, J. G., & Bonifacino, J. S. (2002) · The EMBO Journal · doi:10.1093/emboj/21.11.2557 · Cited by 270
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Michels, G., & Hoppe, U. C. (2008) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2007.08.004 · Cited by 198
Gremer, L., Merbitz-Zahradnik, T., Dvorsky, R., Cirstea, I. C., Kratz, C. P., Zenker, M., Wittinghofer, A., & Ahmadian, M. R. (2011) · Human Mutation · doi:10.1002/humu.21377 · Cited by 158
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Grant, B. D., & Caplan, S. (2008) · Traffic · doi:10.1111/j.1600-0854.2008.00834.x · Cited by 137
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Sakmar, T. P. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00306-x · Cited by 112
Cameron, D. M., Thompson, J., March, P. E., & Dahlberg, A. E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00235-8 · Cited by 99
Jian, X., Tang, W.-K., Zhai, P., Roy, N. S., Luo, R., Gruschus, J. M., Yohe, M. E., Chen, P.-W., Li, Y., Byrd, R. A., et al. (2015) · Structure · doi:10.1016/j.str.2015.08.008 · Cited by 67
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Chung, W.-C., & Kermode, J. C. (2005) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.078311 · Cited by 59
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Dissecting the molecular basis for the modulation of neurotransmitter GPCR signaling by GINIP
Luebbers, A., Gonzalez-Hernandez, A. J., Zhou, M., Eyles, S. J., Levitz, J., & Garcia-Marcos, M. (2024) · Structure · doi:10.1016/j.str.2023.10.010 · Cited by 13
Salama, R., Peet, E., Morrione, T. L., Durant, S., Seager, M., Rennie, M., Scarlata, S., & Nechipurenko, I. (2025) · GENETICS · doi:10.1093/genetics/iyaf216 · Cited by 2
Metadata
- Authors
- Sprang, S. R.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 1997-06
- Volume
- 66
- Issue
- 1
- Pages
- 639-678
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2114460420
- Cited by
- 1,065
- References
- 3
- FWCI
- 3.43
- Type
- journal article
- Language
- en
- Open access
- closed
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