Structural and functional evolution of the P2Y12-like receptor group |
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Authors: | Torsten Schöneberg Thomas Hermsdorf Eva Engemaier Kathrin Engel Ines Liebscher Doreen Thor Klaas Zierau Holger Römpler Angela Schulz |
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Institution: | (1) Institute of Biochemistry, Molecular Biochemistry, Medical Faculty, University of Leipzig, Johannisallee 30, 04103 Leipzig, Germany;(2) Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, MA, USA |
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Abstract: | Metabotropic pyrimidine and purine nucleotide receptors (P2Y receptors) belong to the superfamily of G protein-coupled receptors
(GPCR). They are distinguishable from adenosine receptors (P1) as they bind adenine and/or uracil nucleotide triphosphates
or diphosphates depending on the subtype. Over the past decade, P2Y receptors have been cloned from a variety of tissues and
species, and as many as eight functional subtypes have been characterized. Most recently, several members of the P2Y12-like receptor group, which includes the clopidogrel-sensitive ADP receptor P2Y12, have been deorphanized. The P2Y12-like receptor group comprises several structurally related GPCR which, however, display heterogeneous agonist specificity
including nucleotides, their derivatives, and lipids. Besides the established function of P2Y12 in platelet activation, expression in macrophages, neuronal and glial cells as well as recent results from functional studies
implicate that several members of this group may have specific functions in neurotransmission, inflammation, chemotaxis, and
response to tissue injury. This review focuses specifically on the structure-function relation and shortly summarizes some
aspects of the physiological relevance of P2Y12-like receptor members. |
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Keywords: | Evolution G protein-coupled receptor Nucleotide receptor Orphan GPCR |
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