Among membrane-bound receptors, the seven transmembrane receptors are the most abundant (several thousand, 1% of the genome). They were the most successful during evolution. They are capable of transducing messages as different as photons, organic odorants, nucleotides, nucleosides, peptides, lipids, proteins, etc. They are catalysts of the GDP/GTP nucleotide exchange on heterotrimeric G proteins. They are therefore also called 'G-protein-coupled receptors' (GPCR). G proteins are composed of three subunits, G alpha and two undissociable subunits, G beta gamma. There are at least three families of GPCR showing no sequence similarity. Among G proteins, some have been crystallized (including under the heterotrimeric form) and their structure as well as their activation mechanisms are well known. The structures of GPCR are less known owing to the difficulty in crystallizing membrane-bound proteins. Indirect studies (mutations, 2D crystallization of rhodopsine, molecular modelling, etc.) lead to a useful model of the 'central core' composed of the seven transmembrane domains and of its structural modifications during activation. The intimate contact zones between GPCR and G proteins include, on the GPCR side, domains of intracellular loops and C-terminal, which are specific for each family and on the G protein side, essentially the N- et C-terminal domains plus the alpha 4-beta 6 loop. GPCR can adopt several 'active' conformations some of them being found in mutated receptors responsible for pathologies.