Light on the structure of thromboxane A2 receptor heterodimers
Light on the structure of thromboxane A2 receptor heterodimers
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DOI：
10.1007/s00018-010-0615-0
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发表时间：
2011-09-01
影响因子：
8
通讯作者：
Parenti, Marco
中科院分区：
文献类型：
--
作者：
Fanelli, Francesca;Mauri, Mario;Parenti, Marco
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 TP alpha and beta isoforms are characterized by contacts between hydrophobic residues in helix 1 from both monomers. Functional characterization confirms that TP alpha-TP beta hetero-dimerization serves to regulate TP alpha 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.
