Abstract
Among the functionally very heterogeneous G protein-coupled receptors (GPCR) the EDG (endothelial differentiation gene) proteins define a new class of seven transmembrane proteins. The founding member, EDG1, was isolated as a PMA- inducible immediate-early transcript from human umbilical vein endothelial cells (HUVEC) [1]. Up to now six receptors belonging to the EDG family have been identified (see Table 1). As is typical for GPCRs, EDG receptors share the closest similarities in the sequences encompassing the transmembrane domain 1 (TM1) through TM7. Apart from this, EDG receptors are characterized by distinct sequence features such as a GWN/HC tetrapeptide found at the end of TM4. Furthermore all EDG proteins lack a cysteine residue in the first extracellular loop which is usually part of a disulphide bridge in GPCRs [2].
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Gräler, M.H., Bernhardt, G., Lipp, M. (1999). A Lymphoid Tissue-Specific Receptor, EDG6, with Potential Immune Modulatory Functions Mediated by Extracellular Lysophospholipids. In: Melchers, F., Potter, M. (eds) Mechanisms of B Cell Neoplasia 1998. Current Topics in Microbiology and Immunology, vol 246. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-60162-0_17
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DOI: https://doi.org/10.1007/978-3-642-60162-0_17
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