The structure-based design of a mutant form of the thromboxane A(2) prostanoid receptor (TP) was instrumental in characterizing the structural determinants of the hetero-dimerization process of this G protein coupled receptor (GPCR). The results suggest that the hetero-dimeric complexes between the TPalpha and beta isoforms are characterized by contacts between hydrophobic residues in helix 1 from both monomers. Functional characterization confirms that TPalpha-TPbeta hetero-dimerization serves to regulate TPalpha function through agonist-induced internalization, with important implications in cardiovascular homeostasis. The integrated approach employed in this study can be adopted to gain structural and functional insights into the dimerization/oligomerization process of all GPCRs for which the structural model of the monomer can be achieved at reasonable atomic resolution.

Light on the structure of thromboxane A2 receptor heterodimers / Fanelli, Francesca; M., Mauri; V., Capra; F., Raimondi; F., Guzzi; M., Ambrosio; G. E., Rovati; M., Parenti. - In: CELLULAR AND MOLECULAR LIFE SCIENCES. - ISSN 1420-9071. - ELETTRONICO. - 68(2011), pp. 3109-3120.

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