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Science 12 August 1988:
Vol. 241. no. 4867, pp. 832 - 835
DOI: 10.1126/science.3136547
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Articles

Science, Vol 241, Issue 4867, 832-835
Copyright © 1988 by American Association for the Advancement of Science

articles

Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit

HE Hamm, D Deretic, A Arendt, PA Hargrave, B Koenig, and KP Hofmann

Department of Physiology and Biophysics, University of Illinois College of Medicine, Chicago 60680.

The interaction between receptors and guanine nucleotide binding (G) proteins leads to G protein activation and subsequent regulation of effector enzymes. The molecular basis of receptor-G protein interaction has been examined by using the ability of the G protein from rods (transducin) to cause a conformational change in rhodopsin as an assay. Synthetic peptides corresponding to two regions near the carboxyl terminus of the G protein alpha subunit, Glu311-Val328 and Ile340-Phe350, compete with G protein for interaction with rhodopsin. Amino acid substitution studies show that Cys321 is required for this effect. Ile340-Phe350 and a modified peptide, acetyl-Glu311-Lys329-amide, mimic G protein effects on rhodopsin conformation, showing that these peptides bind to and stabilize the activated conformation of rhodopsin.


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Diversity of G proteins in signal transduction.
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J P Hirsch, C Dietzel, and J Kurjan (1991)
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A monoclonal antibody to the alpha subunit of Gk blocks muscarinic activation of atrial K+ channels.
A Yatani, H Hamm, J Codina, M. Mazzoni, L Birnbaumer, and A. Brown (1988)
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J. Blahos, T. Fischer, I. Brabet, D. Stauffer, G. Rovelli, J. Bockaert, and J.-P. Pin (2001)
J. Biol. Chem. 276, 3262-3269
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