Abstract
The common property of G-binding proteins is, by definition, the ability to bind guanine nucleotides. In this review we shall make our task easier by concentrating on the domain or subunits responsible for carrying out this function. This is not, however, intended to preempt the issue: a common function of such a general nature, exercised in so many different biological organisms and biochemical contexts, does not automatically imply a high, or even a detectable, degree of homology among the proteins that proffer it. Indeed, the G-proteins provide a spectrum of degrees of kinship that range from the intimate to the unrecognizable. Satisfyingly, this spectrum correlates largely with similarity of function, at least within the general classes of G-protein. Nevertheless, between these classes it remains a matter for conjecture whether the difference between just-detectable homology and no detectable homology, significant as it may be in the statistical sense, is significant in the subjective sense of “telling us anything about evolution.”
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© 1990 Plenum Press, New York
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Clark, B.F.C., Jensen, M., Kjeldgaard, M., Thirup, S. (1990). Structural Homologies in G-Binding Proteins. In: Hook, J.B., Poste, G., Schatz, J. (eds) Protein Design and the Development of New Therapeutics and Vaccines. New Horizons in Therapeutics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5739-1_9
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