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Cellular Localization of Seven Transmembrane Domain Receptor mRNA’S by In-Situ Hybridization

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Book cover Biological Signal Transduction

Part of the book series: NATO ASI Series ((ASIH,volume 52))

Abstract

Our research programme involves the study of G-protein coupled, neurotransmitter and neuropeptide receptors, which have been isolated from species specific cDNA libraries, using molecular cloning techniques. The primary structure of a number of G-protein coupled receptors has previously been analysed and it is generally accepted that the members of this receptor superfamily possess a characteristic structure consisting of seven hydrophobic transmembrane domains, generating three cytoplasmic loops, the third of which is the most variable. The extracellular domain probably embodies the ligand recognition site; the cytoplasmic domains are involved in G-protein recognition and coupling, and hence activation of second messenger systems.

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© 1991 Springer-Verlag Berlin Heidelberg

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Peters, T., Taylor, P.L., Eidne, K.A. (1991). Cellular Localization of Seven Transmembrane Domain Receptor mRNA’S by In-Situ Hybridization. In: Ross, E.M., Wirtz, K.W.A. (eds) Biological Signal Transduction. NATO ASI Series, vol 52. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75136-3_9

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  • DOI: https://doi.org/10.1007/978-3-642-75136-3_9

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-75138-7

  • Online ISBN: 978-3-642-75136-3

  • eBook Packages: Springer Book Archive

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