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Characterisation of G-Protein-coupled Receptors by Antibodies

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G-protein-coupled receptors constitute a superfamily of integral membrane proteins encompassing hundreds of receptors for all types of chemical messengers, as well as, for example, the key molecules of our light and smell sensory systems, bioactive amines, peptide hormones, neurotrans-mitters and even proteins. Because of their complicated organisation with the characteristic seven transmembrane segments (7 TM) it has yet been impossible to structurally characterise any G-protein coupled receptor by crystallography or magnetic resonance. However, a number of indirect methods to study the structure and ligand binding of these proteins have been developed. Various studies have shown that antibodies produced against G-protein-coupled receptors are valuable tools. In this review we focus on the use of anti-receptor antibodies for the characterisation of membranes, cells and tissue, for mapping of the binding site, for purification by immunoaffinity chromatography and for biochemical studies of G-protein-coupled receptors. As an example we describe the characterisation of the G-protein-coupled neuropeptide Y receptor subtypes.

Keywords: 3 cholamidoprophyl dimethyl; Anti receptor anitbodies; Antibodies; G protein coupled receptors; Immunofluorescence; Neuropeptide; Neuropeptide Y receptors; aminomethane; enzyme linked immunosorbant assay ELISA; fkyiresceubusituiiocyanate; hydroxymethy; keyhole limpet hemocyanin; neuropeptided y receptors subtypes

Document Type: Review Article


Publication date: 2000-09-01

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  • Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.
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