期刊
TRENDS IN PHARMACOLOGICAL SCIENCES
卷 32, 期 9, 页码 514-520出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tips.2011.05.006
关键词
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资金
- SERVIER
- Fondation pour la Recherche Medicale (Equipe FRM)
- Association pour la Recherche sur le Cancer [5051]
- Institut National de la Sante et de la Recherche Medicale
- Centre National de la Recherche Scientifique
G protein-coupled receptors (GPCRs) can exist as dimers or as larger oligomeric clusters that enable intercommunication between different receptor protomers within the same complex. This phenomenon is observed at three distinct levels: (i) at the level of ligand binding where the activation of one protomer can allosterically inhibit or facilitate ligand binding to the second protomer; (ii) at the level of ligand-induced conformational switches, which occur between transmembrane domains of the two protomers; and (iii) within GPCR-associated protein complexes, either directly at the level of GPCR-interacting proteins or at further downstream levels of the complex. Intercommunication at these different levels introduces asymmetry within GPCR dimers wherein each protomer fulfills its specific task. In this review, we discuss how the asymmetric behavior of GPCRs highlights the advantage of oligomeric receptor organization and supports the functional relevance of GPCR dimerization.
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