Abstract
The heptahelical G protein coupling receptors oligomerize extensively via transmembrane domains, in association with heterotrimeric G proteins. This provides higher affinity for agonists, conformational stability necessary for signal transduction, and protection from intracellular proteinases. The oligomerization is relevant to organismic pathophysiology and could be targeted by natural or modified agonists. For Supplement material, please see the online version of the article.
Keywords: Rhodopsin-like receptor, receptor homodimer, receptor heterodimer, receptor oligomer, signal transduction
Mini-Reviews in Medicinal Chemistry
Title: Oligomerization of the Heptahelical G Protein Coupling Receptors: A Case for Association Using Transmembrane Helices (Supplimentry Material)
Volume: 9 Issue: 3
Author(s): M. S. Parker, R. Sah, E. A. Park, T. Sweatman, A. Balasubramaniam, F. R. Sallee and S. L. Parker
Affiliation:
Keywords: Rhodopsin-like receptor, receptor homodimer, receptor heterodimer, receptor oligomer, signal transduction
Abstract: The heptahelical G protein coupling receptors oligomerize extensively via transmembrane domains, in association with heterotrimeric G proteins. This provides higher affinity for agonists, conformational stability necessary for signal transduction, and protection from intracellular proteinases. The oligomerization is relevant to organismic pathophysiology and could be targeted by natural or modified agonists. For Supplement material, please see the online version of the article.
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Cite this article as:
Parker S. M., Sah R., Park A. E., Sweatman T., Balasubramaniam A., Sallee R. F. and Parker L. S., Oligomerization of the Heptahelical G Protein Coupling Receptors: A Case for Association Using Transmembrane Helices (Supplimentry Material), Mini-Reviews in Medicinal Chemistry 2009; 9 (3) . https://dx.doi.org/10.2174/1389557510909030329
DOI https://dx.doi.org/10.2174/1389557510909030329 |
Print ISSN 1389-5575 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5607 |
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