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- W2044975682 abstract "All three α2-adrenoceptor subtypes have a long third intracellular loop (3i), which is conserved by overall size and charge-hydrophobic properties but not by amino acid sequence similarity. These properties must be relevant for function and structure, because they have been preserved during hundreds of millions of years of evolution. The contribution of different loop portions to agonist/antagonist binding properties and G protein coupling of the human α2B-adrenoceptor (α2B-AR) was investigated with a series of 3i truncated constructs (Δ 3i). We used a variety of agonists/antagonists in competition binding assays. We stimulated α2B-AR Δ3i with various agonists and measured [35S]GTPγS binding in isolated cell membranes with or without antagonist inhibition. We also evaluated the ability of oligopeptides, analogous to the amino and carboxyl terminal parts of 3i, to promote G protein activation, monitored with the [35S]GTPγS assay. Our results reveal that the carboxyl end residues of 3i, R360(6.24) to V372(6.36), are important for Gi/Go protein activation. Deletions in regions from G206(5.72) to R245(5.110) altered the binding of some α2B-AR agonists, indicating that agonist binding is dependent on the conformation of the 3i domain, possibly through the involvement of G protein interactions. The truncated receptor constructs may be more stable on purification and thus be useful for structural characterization of α2B-AR." @default.
- W2044975682 created "2016-06-24" @default.
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- W2044975682 date "2005-01-01" @default.
- W2044975682 modified "2023-10-12" @default.
- W2044975682 title "Intracellularly Truncated Human α2B-Adrenoceptors: Stable and Functional GPCRs for Structural Studies" @default.
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- W2044975682 doi "https://doi.org/10.1081/rrs-200068745" @default.
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