Protein Engineering vol. 1 no. 1 pp. 47-54, 1986
© 1986 Oxford University Press
RESEARCH-ARTICLE |
Family of G protein 
chains: amphipathic analysis and predicted structure of functional domains
1Departments of Pharmacology and Medicine and the Cardiovascular Research Institute, University of California San Francisco, CA 94134, USA 2Department of Biochemistry and Biophysics, University of California San Francisco, CA 94134, USA
The G proteins transduce hormonal and other signals into regulation of enzymes such as adenylyl cyclase and retinal cGMP phosphodiesterase. Each G protein contains an 
subunit that binds and hydrolyzes guanine nucleotides and interacts with ß
subunits and specific receptor and effector proteins. Amphipathic and secondary structure analysis of the primary sequences of five different chains (bovine s, t1 and t2, mouse i, and rat o) predicted the secondary structure of a composite chain (avg). The chains contain four short regions of sequence homologous to regions in the GDP binding domain of bacterial elongation factor Tu (EF-Tu). Similarities between the predicted secondary structures of these regions in avg and the known secondary structure of EF-Tu allowed us to construct a three-dimensional model of the GDP binding domain of avg. Identification of the GDP binding domain of avg defined three additional domains in the composite polypeptide. The first includes the amino terminal 41 residues of avg, with a predicted am phipathic helical structure; this domain may control binding of the chains to the ß complex. The second domain, containing predicted ß strands and helices, several of which are strongly amphipathic, probably contains sequences responsible for interaction of chains with effector enzymes. The predicted structure of the third domain, containing the carhoxy terminal 100 amino acids, is predominantly ß sheet with an amphipathic helix at the carboxy terminus. We propose that this domain is reponsible for receptor binding. Our model should help direct further experiments into the structure and function of the G protein chain.
Keywords: GTP binding proteins/secondary structure/amphipathic analysis/signal transduction/receptors
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