Evidence for multiple biochemically distinguishable states in the G protein-coupled receptor, rhodopsin
Article Abstract:
The basal activities of the rhodopsin receptor are activated by the G protein-coupled receptor in its multi-state conformation. Amino acid substitution of G protein-coupled receptor mutations in specific sites indicated that the receptor can be activated without endogenous stimulus. In addition, the three cytoplasmic loops of the receptor41 is related to the inactive state of rhodopsin, wherein displacement of one or more of these loops result in the lower affinity for the G protein.
Publication Name: Trends in Pharmacological Sciences
Subject: Pharmaceuticals and cosmetics industries
ISSN: 0165-6147
Year: 1998
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G protein interaction with K+ and Ca2+ channels
Article Abstract:
G protein-modulated K+ channels and voltage-dependent Ca2+ channels have a common mechanism for hormonal modulation. The functional interaction of G proteins with these channels appears to be facilitated through G(betagamma). The specificity of this interaction may have been provided by the G(alpha) subunit. Close links between receptor, G protein and channels as effectors enable speedy signal transduction and could be prompted by protein coprocessing through Golgi vesicles.
Publication Name: Trends in Pharmacological Sciences
Subject: Pharmaceuticals and cosmetics industries
ISSN: 0165-6147
Year: 1997
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TinyGRAP database: a bioinformatics tool to mine G-protein-coupled receptor mutant data
Article Abstract:
Research describes a method to collect and disseminate voluminous data on the G-protein-coupled receptors (GPCRs). TinyGRAP database is part of a larger GPCRDB publicy accessible database containing GPCRs data targeted to the professionals in the bioinformatics research.
Publication Name: Trends in Pharmacological Sciences
Subject: Pharmaceuticals and cosmetics industries
ISSN: 0165-6147
Year: 1999
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