A concept for G protein activation by G protein-coupled receptor dimers: the transducin/rhodopsin interface.

TitleA concept for G protein activation by G protein-coupled receptor dimers: the transducin/rhodopsin interface.
Publication TypeJournal Article
Year of Publication2004
AuthorsFilipek, Sławomir, Krzyśko Krystiana A., Fotiadis Dimitrios, Liang Yan, Saperstein David A., Engel Andreas, and Palczewski Krzysztof
JournalPhotochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
Volume3
Issue6
Pagination628-38
Date Published2004 Jun
ISSN1474-905X
KeywordsAnimals, Dimerization, Models, Molecular, Protein Conformation, Protein Structure, Secondary, Receptors, G-Protein-Coupled, Rhodopsin
AbstractG protein-coupled receptors (GPCRs) are ubiquitous and essential in modulating virtually all physiological processes. These receptors share a similar structural design consisting of the seven-transmembrane alpha-helical segments. The active conformations of the receptors are stabilized by an agonist and couple to structurally highly conserved heterotrimeric G proteins. One of the most important unanswered questions is how GPCRs couple to their cognate G proteins. Phototransduction represents an excellent model system for understanding G protein signaling, owing to the high expression of rhodopsin in rod photoreceptors and the multidisciplinary experimental approaches used to study this GPCR. Here, we describe how a G protein (transducin) docks on to an oligomeric GPCR (rhodopsin), revealing structural details of this critical interface in the signal transduction process. This conceptual model takes into account recent structural information on the receptor and G protein, as well as oligomeric states of GPCRs.
DOI10.1039/b315661c
Alternate JournalPhotochem. Photobiol. Sci.
PubMed ID15170495