Abstract
The GDP binding proteins (G-proteins) have attracted much attention in recent years for many good reasons. One good reason is that some of these represent a biomolecular switching mechanism with a possibility of amplification of extracellular signals. Most (if not all) have a specific GDP- binding domain of about 200 residues. This domain can be in an “on-state” complexed with GTP. This state is transformed to the “off-state” by hydrolysis of GTP to GDP. The G-proteins in their “on-state” influence the reactions of other proteins to amplify the signal.
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Nyborg, J., la Cour, T. (1989). New Structural Data on Elongation Factor-Tu:Gdp Based on X-Ray Crystallography. In: Bosch, L., Kraal, B., Parmeggiani, A. (eds) The Guanine — Nucleotide Binding Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2037-2_1
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DOI: https://doi.org/10.1007/978-1-4757-2037-2_1
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