Light on the structure of thromboxane A2 receptor heterodimers |
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Authors: | Francesca Fanelli Mario Mauri Val��rie Capra Francesco Raimondi Francesca Guzzi Manuela Ambrosio G. Enrico Rovati Marco Parenti |
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Affiliation: | Department of Chemistry, Dulbecco Telethon Institute, University of Modena and Reggio Emilia, via Campi 183, 41100 Modena, Italy. fanelli@unimo.it |
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Abstract: | 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 TPα and β isoforms are characterized by contacts between hydrophobic residues in helix 1 from both monomers. Functional characterization confirms that TPα-TPβ hetero-dimerization serves to regulate TPα 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. |
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