期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 68, 期 18, 页码 3109-3120出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-010-0615-0
关键词
GPCR dimerization; Prostanoid receptors; Quaternary structure prediction; Protein-protein docking; Molecular recognition
资金
- Telethon-Italy [S00068TELU]
- Italian Ministry for University and Research (MiUR-FIRB) [RBIN04CKYN]
- European Community [LSHM-CT-2004-005033]
- Fondazione Banca del Monte di Lombardia
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.
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