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The GTPase superfamily: conserved structure and molecular mechanism
Abstract
GTPases are conserved molecular switches, built according to a common structural design. Rapidly accruing knowledge of individual GTPases--crystal structures, biochemical properties, or results of molecular genetic experiments--support and generate hypotheses relating structure to function in other members of the diverse family of GTPases.
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“Rather, due to the intrinsically low GTPase activity of G-proteins, regulatory proteins are required for spatiotemporal control of the transition between active and inactive states (Fig. 1B).”
From RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors (2021) · cites this paper as [8]
In the citing paper
“The affinity of the interaction between GTPases and either guanine nucleotides is extremely high (Kd 10−7–10−11) ensuring that these are committed states that do not spontaneously interchange; they do not respond to changes in cellular nucleotide concentrations (8).”
From RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors (2021) · cites this paper as [8]
In the citing paper
“KRAS proteins primarily bind to guanosine diphosphate (GDP) and are in an inactive conformation maintained by intrinsic guanosine triphosphate (GTP) hydrolytic activity.”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [8]
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Metadata
- Authors
- Bourne, H. R., Sanders, D. A., & McCormick, F.
- Affiliations
- University of California, San Francisco (US)
- Whitehead Institute for Biomedical Research (US)
- Venue
- Nature
- Published
- 1991-01-10
- Volume
- 349
- Issue
- 6305
- Pages
- 117-127
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1977598234
- Cited by
- 3,392
- References
- 149
- Citations by year
- 2026: 24 · 2025: 44 · 2024: 51 · 2023: 52 · 2022: 37 · 2021: 55 · 2020: 62 · 2019: 50 · 2018: 48 · 2017: 44 · 2016: 58 · 2015: 56 · 2014: 63 · 2013: 61 · 2012: 69
- FWCI
- 30.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- GTPase, GTPase superfamily, molecular switches, structure-function relationship, molecular mechanisms, crystal structure, molecular genetics
- MeSH terms
- Amino Acid Sequence, Animals, Guanosine Diphosphate, Guanosine Triphosphate, Humans, Molecular Sequence Data, Peptide Elongation Factors, Peptide Initiation Factors, Protein Conformation, Protein Processing, Post-Translational, Signal Transduction, Proto-Oncogene Proteins p21(ras), GTP-Binding Proteins, GTP Phosphohydrolase-Linked Elongation Factors
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